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 | 0008202 | biological_process | steroid metabolic process |
A | 0008403 | molecular_function | 25-hydroxycholecalciferol-24-hydroxylase 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 | 0033280 | biological_process | response to vitamin D |
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 | 0070643 | molecular_function | vitamin D 25-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 | 0008202 | biological_process | steroid metabolic process |
B | 0008403 | molecular_function | 25-hydroxycholecalciferol-24-hydroxylase 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 | 0033280 | biological_process | response to vitamin D |
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 | 0070643 | molecular_function | vitamin D 25-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: axial binding residue => ECO:0007744|PDB:3K9V, ECO:0007744|PDB:3K9Y |
Chain | Residue | Details |
A | CYS462 | |
B | CYS462 |
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 |