2ZYL
Crystal structure of 3-ketosteroid-9-alpha-hydroxylase (KshA) from M. tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008202 | biological_process | steroid metabolic 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 | 0051536 | molecular_function | iron-sulfur cluster binding |
| 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 | 8 |
| Details | BINDING SITE FOR RESIDUE FES A 451 |
| Chain | Residue |
| A | CYS67 |
| A | HIS69 |
| A | MET70 |
| A | GLY72 |
| A | CYS86 |
| A | PHE88 |
| A | HIS89 |
| A | TRP91 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 A 452 |
| Chain | Residue |
| A | HIS186 |
| A | ASP304 |
| A | HOH561 |
| A | HIS181 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 387 |
| Chain | Residue |
| A | THR177 |
| A | ASP178 |
| A | MET179 |
| A | GLU322 |
| A | ASP323 |
| A | HOH435 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 102 |
| Details | Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19234303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25049233","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"F1CMY8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19234303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25049233","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| A | HIS181 | |
| A | ASP178 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| A | HIS89 |
