4QCK
Crystal structure of 3-ketosteroid-9-alpha-hydroxylase (KshA) from M. tuberculosis in complex with 4-androstene-3,17-dione
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0036200 | molecular_function | 3-ketosteroid 9-alpha-monooxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047086 | molecular_function | ketosteroid monooxygenase activity |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| A | 0070207 | biological_process | protein homotrimerization |
| A | 0070723 | biological_process | response to cholesterol |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 401 |
| Chain | Residue |
| A | ASN175 |
| A | HIS181 |
| A | HIS186 |
| A | ASP304 |
| A | HOH628 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES A 402 |
| Chain | Residue |
| A | CYS86 |
| A | PHE88 |
| A | HIS89 |
| A | TRP91 |
| A | CYS67 |
| A | HIS69 |
| A | MET70 |
| A | GLY72 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 403 |
| Chain | Residue |
| A | ARG21 |
| A | TYR22 |
| A | HIS130 |
| A | HIS132 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ASD A 404 |
| Chain | Residue |
| A | ASN175 |
| A | VAL176 |
| A | HIS186 |
| A | GLN204 |
| A | LEU226 |
| A | ALA230 |
| A | MET238 |
| A | ASN240 |
| A | ASN257 |
| A | GLY300 |
| A | ASP304 |
| A | HOH509 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:25049233 |
| Chain | Residue | Details |
| A | CYS67 | |
| A | HIS69 | |
| A | CYS86 | |
| A | HIS89 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:F1CMY8 |
| Chain | Residue | Details |
| A | ASN175 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:25049233 |
| Chain | Residue | Details |
| A | HIS181 | |
| A | HIS186 | |
| A | ASP304 |
