Uniprot ID: Q70AY8
- Protein: OxyB protein
- Organism: Actinoplanes teichomyceticus
- Length: 398
- Sequence:
MSGDGSPPIHTRRQGFDPADELRAAGTLTKISIGSGADAETTWLAAGHAVVRQVLGDHKRFSTRRRFDRRDEIGGTGVFRPRELVGNLMDYDPPEHTRLRHLLTPGFTQRRMRRLAPRIEEIVTDRLDAMEQAGPPADLIELFADEVPGAVLCELIGVPRDDQAMFLQLCHRHLDASLSARKRAAAGEAFARYLVAMMARERKDPGDGFIGSIVAEHGDTITDEELRGVCVQLMLAGDDNVSGMIGLGVLALLRHPEQIAALRGDDQSADRAVDELIRYLTVPYAPTPRTAVEDVMVADQVIKEGETVLCSLPMANRDRALLPDADRLDVTRTPVPHVAFGHGIHHCLGAALTRLQLRIAYTALWRRFPALQLADPAQEIMFRTSTPAYGLTSLLVAW
Number of chains: 6
| Resolution | 1.90 Å |
|---|---|
| Residue indices (Uniprot), coverage | 6-398 (1-398), 1.00 |
| Difference from Uniprot sequence | expression tag:initiating methionine |
| Mutations (UniProt numbering) | None |
| Insertions | 0insMHHHHHHGKPIPNPLLGLDSTENLYFQGIDPFT |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | A |
| Missing residues | 33ILE-41THR:66ARG-82ARG:174LEU-188GLU |
| Structural gaps | Exists |
| label_asym_ids of heme | B |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| Resolution | 2.50 Å |
|---|---|
| Residue indices (Uniprot), coverage | 6-398 (1-398), 1.00 |
| Difference from Uniprot sequence | expression tag |
| Mutations (UniProt numbering) | None |
| Insertions | 0insGIDPFT |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | A |
| Missing residues | 33ILE-40GLU:66ARG-77GLY |
| Structural gaps | Exists |
| label_asym_ids of heme | C |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| Resolution | 2.50 Å |
|---|---|
| Residue indices (Uniprot), coverage | 7-398 (1-398), 1.00 |
| Difference from Uniprot sequence | conflict |
| Mutations (UniProt numbering) | K59Q, R60Q, F67W, R69P, T76K, V78I, Q163R, A164D, L167M, Q168K, R172G, A180Q, R181K, K182R, A186L, E188D, A189K, A191S, V195L, M198I |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 0.9497 |
| auth_asym_id | A |
| Missing residues | 34GLY-39ALA:67TRP-74GLY |
| Structural gaps | Exists |
| label_asym_ids of heme | E |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.15 Å |
| Resolution | 2.50 Å |
|---|---|
| Residue indices (Uniprot), coverage | 6-398 (1-398), 1.00 |
| Difference from Uniprot sequence | conflict |
| Mutations (UniProt numbering) | K59Q, R60Q, F67W, R69P, T76K, V78I, Q163R, A164D, L167M, Q168K, R172G, A180Q, R181K, K182R, A186L, E188D, A189K, A191S, V195L, M198I |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 0.9497 |
| auth_asym_id | B |
| Missing residues | 34GLY-40GLU:68ASP-73ILE |
| 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 | 2.50 Å |
|---|---|
| Residue indices (Uniprot), coverage | 7-398 (1-398), 1.00 |
| Difference from Uniprot sequence | conflict |
| Mutations (UniProt numbering) | K59Q, R60Q, F67W, R69P, T76K, V78I, Q163R, A164D, L167M, Q168K, R172G, A180Q, R181K, K182R, A186L, E188D, A189K, A191S, V195L, M198I |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 0.9497 |
| auth_asym_id | C |
| Missing residues | 34GLY-40GLU:68ASP-72GLU |
| Structural gaps | Exists |
| label_asym_ids of heme | J |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |
| Resolution | 2.50 Å |
|---|---|
| Residue indices (Uniprot), coverage | 7-398 (1-398), 1.00 |
| Difference from Uniprot sequence | conflict |
| Mutations (UniProt numbering) | K59Q, R60Q, F67W, R69P, T76K, V78I, Q163R, A164D, L167M, Q168K, R172G, A180Q, R181K, K182R, A186L, E188D, A189K, A191S, V195L, M198I |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 0.9497 |
| auth_asym_id | D |
| Missing residues | 34GLY-38ASP:68ASP-72GLU |
| Structural gaps | Exists |
| label_asym_ids of heme | K |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
