2CD8
Crystal structure of YC-17-bound cytochrome P450 PikC (CYP107L1)
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 | 0017000 | biological_process | antibiotic biosynthetic process |
A | 0020037 | molecular_function | heme binding |
A | 0033068 | biological_process | macrolide biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0055114 | biological_process | obsolete oxidation-reduction process |
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 | 0017000 | biological_process | antibiotic biosynthetic process |
B | 0020037 | molecular_function | heme binding |
B | 0033068 | biological_process | macrolide biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0055114 | biological_process | obsolete oxidation-reduction process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEM A 419 |
Chain | Residue |
A | LYS72 |
A | THR248 |
A | LEU251 |
A | ALA293 |
A | THR294 |
A | ARG296 |
A | ALA346 |
A | PHE347 |
A | GLY348 |
A | ILE351 |
A | HIS352 |
A | MET92 |
A | CYS354 |
A | ILE355 |
A | GLY356 |
A | LEU359 |
A | PXI420 |
A | HOH2138 |
A | LEU93 |
A | HIS100 |
A | ARG104 |
A | PHE111 |
A | ALA243 |
A | GLY244 |
A | THR247 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PXI A 420 |
Chain | Residue |
A | TRP74 |
A | GLU85 |
A | LEU88 |
A | ASN89 |
A | LEU93 |
A | GLU94 |
A | PHE178 |
A | VAL179 |
A | VAL242 |
A | ALA243 |
A | VAL290 |
A | SER292 |
A | THR294 |
A | HEM419 |
A | HOH2139 |
site_id | AC3 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM B 419 |
Chain | Residue |
B | MET92 |
B | LEU93 |
B | HIS100 |
B | ARG104 |
B | PHE111 |
B | LEU240 |
B | ALA243 |
B | GLY244 |
B | THR247 |
B | THR248 |
B | LEU251 |
B | PRO289 |
B | ALA293 |
B | THR294 |
B | ARG296 |
B | ALA346 |
B | ILE351 |
B | HIS352 |
B | CYS354 |
B | ILE355 |
B | GLY356 |
B | ALA360 |
B | PXI420 |
B | HOH2102 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PXI B 420 |
Chain | Residue |
B | GLU85 |
B | LEU88 |
B | ASN89 |
B | LEU93 |
B | GLU94 |
B | PHE178 |
B | VAL179 |
B | MET191 |
B | HIS238 |
B | VAL242 |
B | ALA243 |
B | GLU246 |
B | VAL290 |
B | THR294 |
B | ILE395 |
B | HEM419 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHFCIG |
Chain | Residue | Details |
A | PHE347-GLY356 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459 |
Chain | Residue | Details |
A | GLU94 | |
A | ALA187 | |
A | HIS238 | |
B | GLU94 | |
B | ALA187 | |
B | HIS238 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000312|PDB:2C6H, ECO:0000312|PDB:2C7X, ECO:0000312|PDB:2CA0, ECO:0000312|PDB:2CD8, ECO:0000312|PDB:2VZ7, ECO:0000312|PDB:2VZM, ECO:0000312|PDB:2WHW, ECO:0000312|PDB:2WI9, ECO:0000312|PDB:3ZK5, ECO:0000312|PDB:4B7D, ECO:0000312|PDB:4B7S, ECO:0000312|PDB:4BF4 |
Chain | Residue | Details |
A | CYS354 | |
B | CYS354 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
A | GLU246 | |
A | THR247 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
B | GLU246 | |
B | THR247 |