PDB ID: pdb_00004dvq
- Structure of human aldosterone synthase, CYP11B2, in complex with deoxycorticosterone
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.49 Å
- Deposition date: 2012-02-23
Number of assemblies: 2
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 34-502 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 432ARG-437ASN |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | M |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.09 Å |
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 34-502 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 432ARG-437ASN |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | P |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 34-502 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 431ILE-437ASN |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | S |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 34-502 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 431ILE-437ASN |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | V |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| auth_asym_id | E |
|---|---|
| Residue indices (Uniprot) | 34-509 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 431ILE-436ARG |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | Y |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.10 Å |
| auth_asym_id | F |
|---|---|
| Residue indices (Uniprot) | 34-509 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 431ILE-437ASN |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | BA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.09 Å |
Each chain information
| auth_asym_id | G |
|---|---|
| Residue indices (Uniprot) | 34-502 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 431ILE-437ASN |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | EA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.10 Å |
| auth_asym_id | H |
|---|---|
| Residue indices (Uniprot) | 34-502 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 431ILE-437ASN |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | HA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | I |
|---|---|
| Residue indices (Uniprot) | 34-502 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 431ILE-437ASN |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | JA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| auth_asym_id | J |
|---|---|
| Residue indices (Uniprot) | 34-502 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 431ILE-437ASN |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | LA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| auth_asym_id | K |
|---|---|
| Residue indices (Uniprot) | 34-502 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 429LEU-437ASN |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | NA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| auth_asym_id | L |
|---|---|
| Residue indices (Uniprot) | 36-502 (34-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 82ASN-85GLY:431ILE-439HIS |
| Structural gaps | Exists |
| Uniprot ID | P19099 →UniprotKB |
| label_asym_ids of heme | QA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |

