1SMJ
Structure of the A264E mutant of cytochrome P450 BM3 complexed with palmitoleate
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 | 0020037 | molecular_function | heme 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 | 0020037 | molecular_function | heme binding |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0005506 | molecular_function | iron ion binding |
C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
C | 0020037 | molecular_function | heme binding |
D | 0004497 | molecular_function | monooxygenase activity |
D | 0005506 | molecular_function | iron ion binding |
D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
D | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HEM A 472 |
Chain | Residue |
A | LYS69 |
A | THR327 |
A | PHE331 |
A | PRO392 |
A | PHE393 |
A | GLY394 |
A | ARG398 |
A | CYS400 |
A | ILE401 |
A | GLY402 |
A | LEU86 |
A | PHE87 |
A | TRP96 |
A | PHE261 |
A | GLU264 |
A | GLY265 |
A | THR268 |
A | THR269 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE HEM B 472 |
Chain | Residue |
B | LYS69 |
B | LEU86 |
B | PHE87 |
B | TRP96 |
B | GLU264 |
B | GLY265 |
B | THR268 |
B | THR327 |
B | PHE331 |
B | PHE393 |
B | GLY394 |
B | ARG398 |
B | ALA399 |
B | CYS400 |
B | ILE401 |
B | GLY402 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM C 472 |
Chain | Residue |
C | LYS69 |
C | LEU86 |
C | PHE87 |
C | TRP96 |
C | PHE261 |
C | GLU264 |
C | GLY265 |
C | THR268 |
C | THR269 |
C | THR327 |
C | ALA328 |
C | PHE331 |
C | PRO392 |
C | GLY394 |
C | ARG398 |
C | ALA399 |
C | CYS400 |
C | ILE401 |
C | GLY402 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HEM D 472 |
Chain | Residue |
D | LYS69 |
D | LEU86 |
D | PHE87 |
D | TRP96 |
D | PHE261 |
D | GLU264 |
D | GLY265 |
D | THR268 |
D | THR269 |
D | THR327 |
D | ALA328 |
D | PHE331 |
D | PRO392 |
D | ARG398 |
D | CYS400 |
D | ILE401 |
D | GLY402 |
D | PHE405 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PAM A 1465 |
Chain | Residue |
A | VAL26 |
A | TYR51 |
A | VAL78 |
A | PHE87 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PAM B 2465 |
Chain | Residue |
B | TYR51 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PAM C 3465 |
Chain | Residue |
C | TYR51 |
C | PHE87 |
C | LEU188 |
C | ILE263 |
C | GLU264 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PAM D 4465 |
Chain | Residue |
D | LEU20 |
D | TYR51 |
D | PHE87 |
D | LEU188 |
D | THR260 |
D | GLU264 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGnGQRACIG |
Chain | Residue | Details |
A | PHE393-GLY402 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ |
Chain | Residue | Details |
A | LEU52 | |
B | LEU52 | |
C | LEU52 | |
D | LEU52 |
Chain | Residue | Details |
A | ILE401 | |
B | ILE401 | |
C | ILE401 | |
D | ILE401 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Important for catalytic activity => ECO:0000305|PubMed:16403573, ECO:0000305|PubMed:7578081 |
Chain | Residue | Details |
A | THR269 | |
B | THR269 | |
C | THR269 | |
D | THR269 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
A | THR268 | |
A | GLU267 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
B | THR268 | |
B | GLU267 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
C | THR268 | |
C | GLU267 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
D | THR268 | |
D | GLU267 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 699 |
Chain | Residue | Details |
A | THR269 | electrostatic stabiliser, steric role |
A | GLY394 | electrostatic stabiliser, steric role |
A | ILE401 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 699 |
Chain | Residue | Details |
B | THR269 | electrostatic stabiliser, steric role |
B | GLY394 | electrostatic stabiliser, steric role |
B | ILE401 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 699 |
Chain | Residue | Details |
C | THR269 | electrostatic stabiliser, steric role |
C | GLY394 | electrostatic stabiliser, steric role |
C | ILE401 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 3 |
Details | M-CSA 699 |
Chain | Residue | Details |
D | THR269 | electrostatic stabiliser, steric role |
D | GLY394 | electrostatic stabiliser, steric role |
D | ILE401 | electrostatic stabiliser |