3K9V
Crystal structure of rat mitochondrial P450 24A1 S57D in complex with CHAPS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001649 | biological_process | osteoblast differentiation |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006706 | biological_process | steroid catabolic process |
| A | 0008403 | molecular_function | 25-hydroxycholecalciferol-24-hydroxylase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0030342 | molecular_function | 1-alpha,25-dihydroxyvitamin D3 24-hydroxylase activity |
| A | 0030343 | molecular_function | vitamin D3 25-hydroxylase activity |
| A | 0033280 | biological_process | response to vitamin D |
| A | 0036378 | biological_process | calcitriol biosynthetic process from calciol |
| A | 0042359 | biological_process | vitamin D metabolic process |
| A | 0042369 | biological_process | vitamin D catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0062180 | molecular_function | 25-hydroxycholecalciferol-23-hydroxylase activity |
| A | 0062181 | molecular_function | 1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity |
| A | 0070576 | molecular_function | vitamin D 24-hydroxylase activity |
| A | 0071305 | biological_process | cellular response to vitamin D |
| B | 0001649 | biological_process | osteoblast differentiation |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006706 | biological_process | steroid catabolic process |
| B | 0008403 | molecular_function | 25-hydroxycholecalciferol-24-hydroxylase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0030342 | molecular_function | 1-alpha,25-dihydroxyvitamin D3 24-hydroxylase activity |
| B | 0030343 | molecular_function | vitamin D3 25-hydroxylase activity |
| B | 0033280 | biological_process | response to vitamin D |
| B | 0036378 | biological_process | calcitriol biosynthetic process from calciol |
| B | 0042359 | biological_process | vitamin D metabolic process |
| B | 0042369 | biological_process | vitamin D catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0062180 | molecular_function | 25-hydroxycholecalciferol-23-hydroxylase activity |
| B | 0062181 | molecular_function | 1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity |
| B | 0070576 | molecular_function | vitamin D 24-hydroxylase activity |
| B | 0071305 | biological_process | cellular response to vitamin D |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 520 |
| Chain | Residue |
| A | HOH4 |
| A | SER334 |
| A | THR394 |
| A | ARG396 |
| A | PRO454 |
| A | PHE455 |
| A | GLY456 |
| A | ILE457 |
| A | ARG460 |
| A | MET461 |
| A | CYS462 |
| A | ARG128 |
| A | GLY464 |
| A | CPS600 |
| A | LEU147 |
| A | TRP155 |
| A | ARG159 |
| A | LEU323 |
| A | ALA326 |
| A | ALA327 |
| A | THR330 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CPS A 600 |
| Chain | Residue |
| A | SER205 |
| A | ASN208 |
| A | LYS243 |
| A | GLU329 |
| A | THR394 |
| A | GLY499 |
| A | HEM520 |
| A | HOH584 |
| A | HOH597 |
| A | HOH618 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CPS A 601 |
| Chain | Residue |
| A | GLN82 |
| A | PHE104 |
| A | LEU129 |
| A | LYS132 |
| A | MET253 |
| B | LEU66 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CPS A 602 |
| Chain | Residue |
| B | TRP64 |
| B | GLU72 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM B 520 |
| Chain | Residue |
| B | ARG128 |
| B | LEU147 |
| B | TRP155 |
| B | ARG159 |
| B | LEU323 |
| B | ALA326 |
| B | ALA327 |
| B | THR330 |
| B | SER334 |
| B | THR394 |
| B | ARG396 |
| B | PRO454 |
| B | PHE455 |
| B | GLY456 |
| B | ILE457 |
| B | ARG460 |
| B | MET461 |
| B | CYS462 |
| B | GLY464 |
| B | CPS700 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CPS B 700 |
| Chain | Residue |
| B | TYR204 |
| B | MET246 |
| B | GLU329 |
| B | PHE393 |
| B | THR394 |
| B | GLY499 |
| B | HEM520 |
| B | HOH599 |
| B | HOH619 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CPS B 701 |
| Chain | Residue |
| A | LEU66 |
| B | PHE74 |
| B | LEU79 |
| B | PHE104 |
| B | MET253 |
| B | VAL254 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CPS B 702 |
| Chain | Residue |
| A | TRP64 |
| A | TRP75 |
| B | ARG262 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGiGKRMCIG |
| Chain | Residue | Details |
| A | PHE455-GLY464 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PDB","id":"3K9V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K9Y","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | GLU329 | |
| A | THR330 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| B | GLU329 | |
| B | THR330 |
