Uniprot ID: P39597
- Protein: Deferrochelatase
- Organism: Bacillus subtilis (strain 168)
- Length: 416
- Sequence:
MSDEQKKPEQIHRRDILKWGAMAGAAVAIGASGLGGLAPLVQTAAKPSKKDEKEEEQIVPFYGKHQAGITTAHQTYVYFAALDVTAKDKSDIITLFRNWTSLTQMLTSGKKMSAEQRNQYLPPQDTGESADLSPSNLTVTFGFGPGFFEKDGKDRFGLKSKKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFLSGGKNGETPRNLFGFKDGTGNQSTKDDTLMNSIVWIQSGEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSSGAPFGQKKETDPVKLNQIPSNSHVSLAKSTGKQILRRAFSYTEGLDPKTGYMDAGLLFISFQKNPDNQFIPMLKALSAKDALNEYTQTIGSALYACPGGCKKGEYIAQRLLES
Number of chains: 30
| Resolution | 1.90 Å |
|---|---|
| Residue indices (Uniprot), coverage | 1-363 (55-416), 0.87 |
| Difference from Uniprot sequence | conflict:initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | A |
| Missing residues | 56GLY-63GLN |
| Structural gaps | Exists |
| label_asym_ids of heme | C |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |
| Resolution | 1.90 Å |
|---|---|
| Residue indices (Uniprot), coverage | 2-363 (55-416), 0.87 |
| Difference from Uniprot sequence | conflict:initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | B |
| Missing residues | 58LYS-62GLU:119MET-123ASN |
| Structural gaps | Exists |
| label_asym_ids of heme | Z |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Resolution | 1.93 Å |
|---|---|
| Residue indices (Uniprot), coverage | 3-363 (55-416), 0.87 |
| Difference from Uniprot sequence | initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | A |
| label_asym_ids of heme | G |
| Available structure | PDB |
| Resolution | 1.93 Å |
|---|---|
| Residue indices (Uniprot), coverage | 2-362 (55-416), 0.87 |
| Difference from Uniprot sequence | initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | B |
| label_asym_ids of heme | M |
| Available structure | PDB |
| Resolution | 1.93 Å |
|---|---|
| Residue indices (Uniprot), coverage | 2-362 (55-416), 0.87 |
| Difference from Uniprot sequence | initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | C |
| label_asym_ids of heme | Q |
| Available structure | PDB |
| Resolution | 1.93 Å |
|---|---|
| Residue indices (Uniprot), coverage | 2-363 (55-416), 0.87 |
| Difference from Uniprot sequence | initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | D |
| Missing residues | 59MET-61ALA |
| Structural gaps | Exists |
| label_asym_ids of heme | X |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| Resolution | 1.93 Å |
|---|---|
| Residue indices (Uniprot), coverage | 3-362 (55-416), 0.87 |
| Difference from Uniprot sequence | initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | E |
| label_asym_ids of heme | DA |
| Available structure | PDB |
| Resolution | 1.93 Å |
|---|---|
| Residue indices (Uniprot), coverage | 1-363 (55-416), 0.87 |
| Difference from Uniprot sequence | initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | F |
| label_asym_ids of heme | HA |
| Available structure | PDB |
| Resolution | 2.10 Å |
|---|---|
| Residue indices (Uniprot), coverage | 1-363 (55-416), 0.87 |
| Difference from Uniprot sequence | conflict:initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | A |
| label_asym_ids of heme | G |
| Available structure | PDB |
| Resolution | 2.10 Å |
|---|---|
| Residue indices (Uniprot), coverage | 3-363 (55-416), 0.87 |
| Difference from Uniprot sequence | conflict:initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | B |
| label_asym_ids of heme | O |
| Available structure | PDB |
| Resolution | 2.10 Å |
|---|---|
| Residue indices (Uniprot), coverage | 1-363 (55-416), 0.87 |
| Difference from Uniprot sequence | conflict:initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | C |
| label_asym_ids of heme | S |
| Available structure | PDB |
| Resolution | 2.10 Å |
|---|---|
| Residue indices (Uniprot), coverage | 2-362 (55-416), 0.87 |
| Difference from Uniprot sequence | conflict:initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | D |
| label_asym_ids of heme | Z |
| Available structure | PDB |
| Resolution | 2.10 Å |
|---|---|
| Residue indices (Uniprot), coverage | 2-363 (55-416), 0.87 |
| Difference from Uniprot sequence | conflict:initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | E |
| label_asym_ids of heme | EA |
| Available structure | PDB |
| Resolution | 2.10 Å |
|---|---|
| Residue indices (Uniprot), coverage | 3-362 (55-416), 0.87 |
| Difference from Uniprot sequence | conflict:initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | F |
| label_asym_ids of heme | KA |
| Available structure | PDB |
| Resolution | 2.10 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (1-416), 1.00 |
| Difference from Uniprot sequence | engineered mutation |
| Mutations (UniProt numbering) | K317E, S325P, A330V |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 0.9928 |
| auth_asym_id | A |
| Missing residues | 309GLN-321ILE |
| Structural gaps | Exists |
| label_asym_ids of heme | E |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.10 Å |
| Resolution | 2.10 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (1-416), 1.00 |
| Difference from Uniprot sequence | engineered mutation |
| Mutations (UniProt numbering) | K317E, S325P, A330V |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 0.9928 |
| auth_asym_id | B |
| Missing residues | 112MET-116GLN:309GLN-321ILE |
| Structural gaps | Exists |
| label_asym_ids of heme | F |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| Resolution | 2.10 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (1-416), 1.00 |
| Difference from Uniprot sequence | engineered mutation |
| Mutations (UniProt numbering) | K317E, S325P, A330V |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 0.9928 |
| auth_asym_id | C |
| Missing residues | 114ALA-115GLU:309GLN-321ILE |
| Structural gaps | Exists |
| label_asym_ids of heme | G |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| Resolution | 2.10 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (1-416), 1.00 |
| Difference from Uniprot sequence | engineered mutation |
| Mutations (UniProt numbering) | K317E, S325P, A330V |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 0.9928 |
| auth_asym_id | D |
| Missing residues | 112MET-116GLN:317GLU-321ILE |
| Structural gaps | Exists |
| label_asym_ids of heme | H |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| Resolution | 2.44 Å |
|---|---|
| Residue indices (Uniprot), coverage | 3-363 (55-416), 0.87 |
| Difference from Uniprot sequence | initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | A |
| label_asym_ids of heme | E |
| Available structure | PDB |
| Resolution | 2.44 Å |
|---|---|
| Residue indices (Uniprot), coverage | 1-363 (55-416), 0.87 |
| Difference from Uniprot sequence | initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | B |
| label_asym_ids of heme | I |
| Available structure | PDB |
| Resolution | 2.44 Å |
|---|---|
| Residue indices (Uniprot), coverage | 2-363 (55-416), 0.87 |
| Difference from Uniprot sequence | initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | C |
| label_asym_ids of heme | M |
| Available structure | PDB |
| Resolution | 2.44 Å |
|---|---|
| Residue indices (Uniprot), coverage | 1-363 (55-416), 0.87 |
| Difference from Uniprot sequence | initiating methionine |
| Mutations (UniProt numbering) | D88E, G146S, K248E, T251S, I259V, V284I |
| Insertions | None |
| Deletions | S2-E54 |
| Sequence identity to UniProt | 0.9835 |
| auth_asym_id | D |
| label_asym_ids of heme | O |
| Available structure | PDB |
| Resolution | 2.49 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (1-416), 1.00 |
| Mutations (UniProt numbering) | None |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | A |
| Missing residues | 112MET-116GLN |
| Structural gaps | Exists |
| label_asym_ids of heme | C |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.10 Å |
| Resolution | 2.49 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (1-416), 1.00 |
| Mutations (UniProt numbering) | None |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | B |
| Missing residues | 111LYS-116GLN |
| Structural gaps | Exists |
| label_asym_ids of heme | D |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.15 Å |
| Resolution | 2.67 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (56-414), 0.86 |
| Difference from Uniprot sequence | variant |
| Mutations (UniProt numbering) | N244L |
| Insertions | None |
| Deletions | M1-E55, E415-S416 |
| Sequence identity to UniProt | 0.9972 |
| auth_asym_id | A |
| Missing residues | 112MET-116GLN |
| Structural gaps | Exists |
| label_asym_ids of heme | G |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Resolution | 2.67 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (56-414), 0.86 |
| Difference from Uniprot sequence | variant |
| Mutations (UniProt numbering) | N244L |
| Insertions | None |
| Deletions | M1-E55, E415-S416 |
| Sequence identity to UniProt | 0.9972 |
| auth_asym_id | B |
| Missing residues | 112MET-116GLN |
| Structural gaps | Exists |
| label_asym_ids of heme | H |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Resolution | 2.67 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (56-414), 0.86 |
| Difference from Uniprot sequence | variant |
| Mutations (UniProt numbering) | N244L |
| Insertions | None |
| Deletions | M1-E55, E415-S416 |
| Sequence identity to UniProt | 0.9972 |
| auth_asym_id | C |
| Missing residues | 112MET-116GLN |
| Structural gaps | Exists |
| label_asym_ids of heme | I |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |
| Resolution | 2.67 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (56-414), 0.86 |
| Difference from Uniprot sequence | variant |
| Mutations (UniProt numbering) | N244L |
| Insertions | None |
| Deletions | M1-E55, E415-S416 |
| Sequence identity to UniProt | 0.9972 |
| auth_asym_id | D |
| Missing residues | 112MET-117ARG |
| Structural gaps | Exists |
| label_asym_ids of heme | J |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| Resolution | 2.67 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (56-414), 0.86 |
| Difference from Uniprot sequence | variant |
| Mutations (UniProt numbering) | N244L |
| Insertions | None |
| Deletions | M1-E55, E415-S416 |
| Sequence identity to UniProt | 0.9972 |
| auth_asym_id | E |
| Missing residues | 112MET-116GLN |
| Structural gaps | Exists |
| label_asym_ids of heme | K |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Resolution | 2.67 Å |
|---|---|
| Residue indices (Uniprot), coverage | 56-414 (56-414), 0.86 |
| Difference from Uniprot sequence | variant |
| Mutations (UniProt numbering) | N244L |
| Insertions | None |
| Deletions | M1-E55, E415-S416 |
| Sequence identity to UniProt | 0.9972 |
| auth_asym_id | F |
| Missing residues | 112MET-116GLN |
| Structural gaps | Exists |
| label_asym_ids of heme | L |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.15 Å |
