Uniprot ID: P08686
- Protein: Steroid 21-hydroxylase
- Organism: Human (Homo sapiens)
- Length: 495
- Sequence:
MLLLGLLLLLPLLAGARLLWNWWKLRSLHLPPLAPGFLHLLQPDLPIYLLGLTQKFGPIYRLHLGLQDVVVLNSKRTIEEAMVKKWADFAGRPEPLTYKLVSRNYPDLSLGDYSLLWKAHKKLTRSALLLGIRDSMEPVVEQLTQEFCERMRAQPGTPVAIEEEFSLLTCSIICYLTFGDKIKDDNLMPAYYKCIQEVLKTWSHWSIQIVDVIPFLRFFPNPGLRRLKQAIEKRDHIVEMQLRQHKESLVAGQWRDMMDYMLQGVAQPSMEEGSGQLLEGHVHMAAVDLLIGGTETTANTLSWAVVFLLHHPEIQQRLQEELDHELGPGASSSRVPYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTRPSSISGYDIPEGTVIIPNLQGAHLDETVWERPHEFWPDRFLEPGKNSRALAFGCGARVCLGEPLARLELFVVLTRLLQAFTLLPSGDALPSLQPLPHCSVILKMQPFQVRLQPRGMGAHSPGQSQ
Number of chains: 6
| Resolution | 2.64 Å |
|---|---|
| Residue indices (Uniprot), coverage | 29-485 (30-495), 0.96 |
| Difference from Uniprot sequence | expression tag:initiating methionine |
| Mutations (UniProt numbering) | N21A, W22K, W23K, K24T, L25S, R26S, S27K, L28G, H29K |
| Insertions | 495insHHHHHH |
| Deletions | L2-W20 |
| Sequence identity to UniProt | 0.9811 |
| auth_asym_id | A |
| Missing residues | 267GLN-275GLY:327GLY-332SER:412GLU-413PRO |
| Structural gaps | Exists |
| label_asym_ids of heme | F |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Resolution | 2.64 Å |
|---|---|
| Residue indices (Uniprot), coverage | 29-484 (30-495), 0.96 |
| Difference from Uniprot sequence | expression tag:initiating methionine |
| Mutations (UniProt numbering) | N21A, W22K, W23K, K24T, L25S, R26S, S27K, L28G, H29K |
| Insertions | 495insHHHHHH |
| Deletions | L2-W20 |
| Sequence identity to UniProt | 0.9811 |
| auth_asym_id | B |
| Missing residues | 268PRO-275GLY:325GLU-332SER |
| Structural gaps | Exists |
| label_asym_ids of heme | I |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Resolution | 2.64 Å |
|---|---|
| Residue indices (Uniprot), coverage | 29-485 (30-495), 0.96 |
| Difference from Uniprot sequence | expression tag:initiating methionine |
| Mutations (UniProt numbering) | N21A, W22K, W23K, K24T, L25S, R26S, S27K, L28G, H29K |
| Insertions | 495insHHHHHH |
| Deletions | L2-W20 |
| Sequence identity to UniProt | 0.9811 |
| auth_asym_id | C |
| Missing residues | 267GLN-274SER:326LEU-332SER |
| Structural gaps | Exists |
| label_asym_ids of heme | L |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| Resolution | 3.31 Å |
|---|---|
| Residue indices (Uniprot), coverage | 29-485 (30-495), 0.96 |
| Difference from Uniprot sequence | expression tag:initiating methionine |
| Mutations (UniProt numbering) | N21A, W22K, W23K, K24T, L25S, R26S, S27K, L28G, H29K |
| Insertions | None |
| Deletions | L2-W20 |
| Sequence identity to UniProt | 0.9811 |
| auth_asym_id | A |
| Missing residues | 267GLN-274SER:326LEU-332SER |
| Structural gaps | Exists |
| label_asym_ids of heme | D |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Resolution | 3.31 Å |
|---|---|
| Residue indices (Uniprot), coverage | 29-484 (30-495), 0.96 |
| Difference from Uniprot sequence | expression tag:initiating methionine |
| Mutations (UniProt numbering) | N21A, W22K, W23K, K24T, L25S, R26S, S27K, L28G, H29K |
| Insertions | None |
| Deletions | L2-W20 |
| Sequence identity to UniProt | 0.9811 |
| auth_asym_id | B |
| Missing residues | 267GLN-274SER:326LEU-332SER |
| Structural gaps | Exists |
| label_asym_ids of heme | F |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Resolution | 3.31 Å |
|---|---|
| Residue indices (Uniprot), coverage | 29-485 (30-495), 0.96 |
| Difference from Uniprot sequence | expression tag:initiating methionine |
| Mutations (UniProt numbering) | N21A, W22K, W23K, K24T, L25S, R26S, S27K, L28G, H29K |
| Insertions | None |
| Deletions | L2-W20 |
| Sequence identity to UniProt | 0.9811 |
| auth_asym_id | C |
| Missing residues | 267GLN-274SER:326LEU-332SER |
| Structural gaps | Exists |
| label_asym_ids of heme | H |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
