5E9Z
Cytochrome P450 BM3 mutant M11
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 | 3 |
Details | binding site for residue FE2 A 501 |
Chain | Residue |
A | CYS400 |
A | PP9502 |
A | HOH778 |
site_id | AC2 |
Number of Residues | 23 |
Details | binding site for residue PP9 A 502 |
Chain | Residue |
A | GLY265 |
A | THR268 |
A | PHE331 |
A | PRO392 |
A | PHE393 |
A | GLY394 |
A | ARG398 |
A | ALA399 |
A | CYS400 |
A | ILE401 |
A | GLY402 |
A | FE2501 |
A | HOH613 |
A | HOH633 |
A | HOH659 |
A | HOH678 |
A | HOH778 |
A | LYS69 |
A | LEU75 |
A | LEU86 |
A | VAL87 |
A | TRP96 |
A | ALA264 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue DTT B 501 |
Chain | Residue |
A | CYS198 |
A | ASN201 |
B | ALA197 |
B | CYS198 |
site_id | AC4 |
Number of Residues | 26 |
Details | binding site for residue PP9 B 502 |
Chain | Residue |
B | LYS69 |
B | LEU86 |
B | VAL87 |
B | TRP96 |
B | PHE107 |
B | ILE153 |
B | ALA264 |
B | GLY265 |
B | THR268 |
B | THR269 |
B | ALA328 |
B | PHE331 |
B | PRO392 |
B | PHE393 |
B | GLY394 |
B | ARG398 |
B | ALA399 |
B | CYS400 |
B | ILE401 |
B | GLY402 |
B | FE2503 |
B | HOH601 |
B | HOH608 |
B | HOH610 |
B | HOH630 |
B | HOH662 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue FE2 B 503 |
Chain | Residue |
B | CYS400 |
B | PP9502 |
B | HOH793 |
site_id | AC6 |
Number of Residues | 28 |
Details | binding site for residue PP9 C 501 |
Chain | Residue |
C | LYS69 |
C | LEU86 |
C | VAL87 |
C | TRP96 |
C | PHE107 |
C | PHE261 |
C | ALA264 |
C | GLY265 |
C | THR268 |
C | THR269 |
C | THR327 |
C | ALA328 |
C | PHE331 |
C | PRO392 |
C | PHE393 |
C | GLY394 |
C | ARG398 |
C | ALA399 |
C | CYS400 |
C | ILE401 |
C | GLY402 |
C | FE2502 |
C | HOH602 |
C | HOH611 |
C | HOH629 |
C | HOH642 |
C | HOH651 |
C | HOH691 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue FE2 C 502 |
Chain | Residue |
C | CYS400 |
C | PP9501 |
C | HOH691 |
site_id | AC8 |
Number of Residues | 24 |
Details | binding site for residue PP9 D 501 |
Chain | Residue |
D | ALA328 |
D | PHE331 |
D | PRO392 |
D | PHE393 |
D | GLY394 |
D | ARG398 |
D | ALA399 |
D | CYS400 |
D | ILE401 |
D | FE2502 |
D | HOH602 |
D | HOH607 |
D | HOH641 |
D | HOH674 |
D | HOH763 |
D | LYS69 |
D | LEU86 |
D | VAL87 |
D | TRP96 |
D | PHE107 |
D | PHE261 |
D | ALA264 |
D | GLY265 |
D | THR268 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue FE2 D 502 |
Chain | Residue |
D | CYS400 |
D | PP9501 |
D | HOH763 |
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 | TYR51 | |
B | TYR51 | |
C | TYR51 | |
D | TYR51 |
Chain | Residue | Details |
A | CYS400 | |
B | CYS400 | |
C | CYS400 | |
D | CYS400 |
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 | THR268 | |
B | THR268 | |
C | THR268 | |
D | THR268 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 699 |
Chain | Residue | Details |
A | THR268 | electrostatic stabiliser, steric role |
A | PHE393 | electrostatic stabiliser, steric role |
A | CYS400 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 699 |
Chain | Residue | Details |
B | THR268 | electrostatic stabiliser, steric role |
B | PHE393 | electrostatic stabiliser, steric role |
B | CYS400 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 699 |
Chain | Residue | Details |
C | THR268 | electrostatic stabiliser, steric role |
C | PHE393 | electrostatic stabiliser, steric role |
C | CYS400 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 3 |
Details | M-CSA 699 |
Chain | Residue | Details |
D | THR268 | electrostatic stabiliser, steric role |
D | PHE393 | electrostatic stabiliser, steric role |
D | CYS400 | electrostatic stabiliser |