3NC3
CYP134A1 structure with a closed substrate binding loop
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0016713 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen |
A | 0020037 | molecular_function | heme binding |
A | 0046148 | biological_process | pigment biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
B | 0016713 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen |
B | 0020037 | molecular_function | heme binding |
B | 0046148 | biological_process | pigment biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM A 406 |
Chain | Residue |
A | LYS62 |
A | ARG285 |
A | ALA345 |
A | PHE346 |
A | HIS351 |
A | CYS353 |
A | VAL354 |
A | GLY355 |
A | PHE358 |
A | ALA359 |
A | ILE363 |
A | ILE97 |
A | GOL407 |
A | HOH428 |
A | MET143 |
A | ASN229 |
A | ALA233 |
A | ALA234 |
A | PRO237 |
A | THR241 |
A | ILE283 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 407 |
Chain | Residue |
A | ASN229 |
A | TYR391 |
A | HEM406 |
A | HOH428 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 408 |
Chain | Residue |
A | ASN252 |
A | GLU254 |
B | ARG342 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG A 409 |
Chain | Residue |
A | LYS277 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 410 |
Chain | Residue |
A | PRO172 |
A | ARG175 |
B | ASN114 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 411 |
Chain | Residue |
A | HIS248 |
A | ASN251 |
A | ASN252 |
site_id | AC7 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE HEM B 406 |
Chain | Residue |
B | SER63 |
B | LEU64 |
B | MET143 |
B | ASN229 |
B | ALA233 |
B | ALA234 |
B | PRO237 |
B | THR241 |
B | ILE283 |
B | ARG285 |
B | ALA345 |
B | HIS351 |
B | CYS353 |
B | VAL354 |
B | GLY355 |
B | PHE358 |
B | ALA359 |
B | ILE363 |
B | GOL407 |
B | HOH431 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 407 |
Chain | Residue |
B | LEU64 |
B | ALA233 |
B | VAL280 |
B | TYR391 |
B | THR392 |
B | HEM406 |
B | HOH431 |
B | HOH432 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 408 |
Chain | Residue |
B | HIS248 |
B | ASN251 |
B | ASN252 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 409 |
Chain | Residue |
B | SER63 |
B | VAL65 |
B | ASN229 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGsGIHNCVG |
Chain | Residue | Details |
A | PHE346-GLY355 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20690619 |
Chain | Residue | Details |
A | LYS62 | |
A | ASN229 | |
A | ARG285 | |
B | LYS62 | |
B | ASN229 | |
B | ARG285 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | CYS353 | |
B | CYS353 |