4QDF
Crystal structure of apo KshA5 and KshA1 in complex with 1,4-30Q-CoA from R. rhodochrous
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| 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 | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0008203 | biological_process | cholesterol metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0036200 | molecular_function | 3-ketosteroid 9-alpha-monooxygenase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES A 401 |
| Chain | Residue |
| A | CYS73 |
| A | HIS75 |
| A | MET76 |
| A | GLY78 |
| A | CYS92 |
| A | HIS95 |
| A | TRP97 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 402 |
| Chain | Residue |
| A | ASP311 |
| A | HOH602 |
| A | HOH621 |
| A | HIS187 |
| A | HIS192 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | GLU236 |
| A | THR238 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PG4 A 404 |
| Chain | Residue |
| A | ARG30 |
| A | GLY31 |
| A | TRP32 |
| A | TRP135 |
| A | VAL147 |
| A | THR148 |
| A | PHE240 |
| A | GLY241 |
| A | PRO242 |
| A | GLN342 |
| A | PHE343 |
| A | ILE350 |
| A | GLU352 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 B 401 |
| Chain | Residue |
| B | HIS181 |
| B | HIS186 |
| B | ASP305 |
| B | HOH533 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES B 402 |
| Chain | Residue |
| B | CYS68 |
| B | HIS70 |
| B | MET71 |
| B | GLY73 |
| B | CYS87 |
| B | HIS90 |
| B | TRP92 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 30Q B 403 |
| Chain | Residue |
| B | ASN175 |
| B | ILE176 |
| B | HIS186 |
| B | GLN204 |
| B | SER229 |
| B | MET239 |
| B | ASP241 |
| B | LEU243 |
| B | TYR245 |
| B | ASP305 |
| B | HOH513 |
| B | HOH533 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 404 |
| Chain | Residue |
| B | PHE23 |
| B | PHE47 |
| B | ARG116 |
| B | HIS131 |
| B | HOH564 |
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:25049233 |
| Chain | Residue | Details |
| B | CYS68 | |
| B | HIS70 | |
| B | CYS87 | |
| B | HIS90 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:F1CMY8 |
| Chain | Residue | Details |
| B | ASN175 | |
| B | HIS181 | |
| A | HIS192 | |
| A | ASP311 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25049233 |
| Chain | Residue | Details |
| B | HIS186 | |
| B | TYR245 | |
| B | ASP305 |
