3QZ1
Crystal Structure of Bovine Steroid of 21-hydroxylase (P450c21)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0004509 | molecular_function | steroid 21-monooxygenase activity |
| A | 0005496 | molecular_function | steroid binding |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006704 | biological_process | glucocorticoid biosynthetic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0103069 | molecular_function | 17-hydroxyprogesterone 21-hydroxylase activity |
| A | 0106309 | molecular_function | progesterone 21-hydroxylase activity |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0004509 | molecular_function | steroid 21-monooxygenase activity |
| B | 0005496 | molecular_function | steroid binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006694 | biological_process | steroid biosynthetic process |
| B | 0006704 | biological_process | glucocorticoid biosynthetic process |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0008395 | molecular_function | steroid hydroxylase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0103069 | molecular_function | 17-hydroxyprogesterone 21-hydroxylase activity |
| B | 0106309 | molecular_function | progesterone 21-hydroxylase activity |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0004509 | molecular_function | steroid 21-monooxygenase activity |
| C | 0005496 | molecular_function | steroid binding |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005789 | cellular_component | endoplasmic reticulum membrane |
| C | 0006694 | biological_process | steroid biosynthetic process |
| C | 0006704 | biological_process | glucocorticoid biosynthetic process |
| C | 0008202 | biological_process | steroid metabolic process |
| C | 0008395 | molecular_function | steroid hydroxylase activity |
| C | 0016020 | cellular_component | membrane |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0103069 | molecular_function | 17-hydroxyprogesterone 21-hydroxylase activity |
| C | 0106309 | molecular_function | progesterone 21-hydroxylase activity |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0004509 | molecular_function | steroid 21-monooxygenase activity |
| D | 0005496 | molecular_function | steroid binding |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005789 | cellular_component | endoplasmic reticulum membrane |
| D | 0006694 | biological_process | steroid biosynthetic process |
| D | 0006704 | biological_process | glucocorticoid biosynthetic process |
| D | 0008202 | biological_process | steroid metabolic process |
| D | 0008395 | molecular_function | steroid hydroxylase activity |
| D | 0016020 | cellular_component | membrane |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0103069 | molecular_function | 17-hydroxyprogesterone 21-hydroxylase activity |
| D | 0106309 | molecular_function | progesterone 21-hydroxylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | ARG92 |
| A | LEU352 |
| A | ALA361 |
| A | LEU362 |
| A | HIS364 |
| A | LEU387 |
| A | ALA419 |
| A | PHE420 |
| A | ARG425 |
| A | VAL426 |
| A | CYS427 |
| A | ILE108 |
| A | LEU428 |
| A | GLY429 |
| A | ALA433 |
| A | 3QZ501 |
| A | SER109 |
| A | TRP117 |
| A | LEU128 |
| A | GLY291 |
| A | THR294 |
| A | THR295 |
| A | THR298 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 3QZ A 501 |
| Chain | Residue |
| A | LEU110 |
| A | LEU196 |
| A | TRP200 |
| A | ARG232 |
| A | GLY290 |
| A | THR294 |
| A | VAL358 |
| A | HEM500 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 3QZ A 502 |
| Chain | Residue |
| A | LEU64 |
| A | GLN67 |
| A | ILE95 |
| A | GLN206 |
| A | VAL382 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM B 500 |
| Chain | Residue |
| B | ARG92 |
| B | ILE108 |
| B | SER109 |
| B | TRP117 |
| B | LYS121 |
| B | LEU128 |
| B | GLY291 |
| B | THR294 |
| B | THR295 |
| B | THR298 |
| B | VAL358 |
| B | LEU362 |
| B | HIS364 |
| B | LEU387 |
| B | ALA419 |
| B | PHE420 |
| B | ARG425 |
| B | CYS427 |
| B | LEU428 |
| B | GLY429 |
| B | ALA433 |
| B | 3QZ501 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 3QZ B 501 |
| Chain | Residue |
| B | SER109 |
| B | LEU110 |
| B | LEU196 |
| B | TRP200 |
| B | ILE229 |
| B | ARG232 |
| B | GLY290 |
| B | THR294 |
| B | VAL358 |
| B | VAL469 |
| B | HEM500 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 3QZ B 502 |
| Chain | Residue |
| B | LEU40 |
| B | LEU64 |
| B | GLN206 |
| B | MET210 |
| B | LEU360 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM C 500 |
| Chain | Residue |
| C | ARG92 |
| C | ILE108 |
| C | SER109 |
| C | GLY291 |
| C | THR294 |
| C | THR295 |
| C | THR298 |
| C | LEU352 |
| C | VAL358 |
| C | HIS364 |
| C | LEU387 |
| C | ALA419 |
| C | PHE420 |
| C | ARG425 |
| C | CYS427 |
| C | LEU428 |
| C | GLY429 |
| C | ALA433 |
| C | 3QZ501 |
| C | HOH606 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 3QZ C 501 |
| Chain | Residue |
| C | ARG232 |
| C | ASP286 |
| C | THR294 |
| C | HEM500 |
| C | VAL101 |
| C | SER109 |
| C | LEU196 |
| C | TRP200 |
| C | ILE229 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 3QZ C 502 |
| Chain | Residue |
| C | GLN206 |
| C | LEU360 |
| C | ALA361 |
| C | CYS467 |
| C | GLY468 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM D 500 |
| Chain | Residue |
| D | ARG92 |
| D | SER109 |
| D | TRP117 |
| D | LYS121 |
| D | GLY291 |
| D | THR294 |
| D | THR295 |
| D | THR298 |
| D | VAL358 |
| D | ALA361 |
| D | HIS364 |
| D | LEU387 |
| D | ALA419 |
| D | PHE420 |
| D | ARG425 |
| D | VAL426 |
| D | CYS427 |
| D | LEU428 |
| D | GLY429 |
| D | 3QZ501 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 3QZ D 501 |
| Chain | Residue |
| D | SER109 |
| D | LEU196 |
| D | TRP200 |
| D | ARG232 |
| D | ASP286 |
| D | THR294 |
| D | HEM500 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 3QZ D 502 |
| Chain | Residue |
| D | LEU64 |
| D | GLY65 |
| D | GLN206 |
| D | LEU360 |
| D | ALA361 |
| D | CYS467 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGcGARVCLG |
| Chain | Residue | Details |
| A | PHE420-GLY429 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22262854, ECO:0007744|PDB:3QZ1 |
| Chain | Residue | Details |
| A | SER109 | |
| D | SER109 | |
| D | HIS364 | |
| D | ARG425 | |
| A | HIS364 | |
| A | ARG425 | |
| B | SER109 | |
| B | HIS364 | |
| B | ARG425 | |
| C | SER109 | |
| C | HIS364 | |
| C | ARG425 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P08686 |
| Chain | Residue | Details |
| A | ARG232 | |
| B | ARG232 | |
| C | ARG232 | |
| D | ARG232 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:22262854, ECO:0007744|PDB:3QZ1 |
| Chain | Residue | Details |
| A | CYS427 | |
| B | CYS427 | |
| C | CYS427 | |
| D | CYS427 |
