5XA3
Crystal Structure of P450BM3 with Benzyloxycarbonyl-L-prolyl-L-phenylalanine
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 | 24 |
Details | binding site for residue HEM A 501 |
Chain | Residue |
A | LYS69 |
A | PHE331 |
A | PRO392 |
A | PHE393 |
A | GLY394 |
A | ARG398 |
A | ALA399 |
A | CYS400 |
A | ILE401 |
A | DMS502 |
A | PHQ503 |
A | LEU86 |
A | HOH604 |
A | HOH615 |
A | HOH630 |
A | HOH637 |
A | HOH686 |
A | PHE87 |
A | TRP96 |
A | ILE153 |
A | ALA264 |
A | THR268 |
A | THR269 |
A | THR327 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue DMS A 502 |
Chain | Residue |
A | PHE87 |
A | ALA264 |
A | THR268 |
A | ALA328 |
A | HEM501 |
site_id | AC3 |
Number of Residues | 24 |
Details | binding site for residue HEM B 501 |
Chain | Residue |
B | LYS69 |
B | LEU86 |
B | PHE87 |
B | TRP96 |
B | ILE153 |
B | ALA264 |
B | THR268 |
B | THR269 |
B | THR327 |
B | PHE331 |
B | PRO392 |
B | PHE393 |
B | GLY394 |
B | ARG398 |
B | ALA399 |
B | CYS400 |
B | ILE401 |
B | DMS502 |
B | PHQ503 |
B | HOH604 |
B | HOH621 |
B | HOH628 |
B | HOH639 |
B | HOH675 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue DMS B 502 |
Chain | Residue |
B | ALA264 |
B | THR268 |
B | HEM501 |
site_id | AC5 |
Number of Residues | 25 |
Details | binding site for residue HEM C 501 |
Chain | Residue |
C | LYS69 |
C | LEU86 |
C | PHE87 |
C | TRP96 |
C | ILE153 |
C | ALA264 |
C | THR268 |
C | THR269 |
C | THR327 |
C | PHE331 |
C | PRO392 |
C | PHE393 |
C | GLY394 |
C | ARG398 |
C | ALA399 |
C | CYS400 |
C | ILE401 |
C | ALA406 |
C | DMS502 |
C | PHQ503 |
C | HOH626 |
C | HOH627 |
C | HOH636 |
C | HOH658 |
C | HOH662 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue DMS C 502 |
Chain | Residue |
C | PHE87 |
C | ALA264 |
C | THR268 |
C | HEM501 |
site_id | AC7 |
Number of Residues | 25 |
Details | binding site for residue HEM D 501 |
Chain | Residue |
D | ALA399 |
D | CYS400 |
D | ILE401 |
D | GLY402 |
D | DMS502 |
D | PHQ503 |
D | HOH608 |
D | HOH625 |
D | HOH633 |
D | HOH638 |
D | HOH699 |
D | LYS69 |
D | LEU86 |
D | PHE87 |
D | TRP96 |
D | ILE153 |
D | ALA264 |
D | THR268 |
D | THR269 |
D | THR327 |
D | PHE331 |
D | PRO392 |
D | PHE393 |
D | GLY394 |
D | ARG398 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue DMS D 502 |
Chain | Residue |
D | PHE87 |
D | ALA264 |
D | THR268 |
D | HEM501 |
site_id | AC9 |
Number of Residues | 10 |
Details | binding site for Di-peptide PRO A 504 and PHQ A 503 |
Chain | Residue |
A | TYR51 |
A | SER72 |
A | ALA74 |
A | LEU75 |
A | PHE87 |
A | ALA330 |
A | MET354 |
A | LEU437 |
A | HEM501 |
A | PHE505 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for Di-peptide PRO A 504 and PHE A 505 |
Chain | Residue |
A | LEU20 |
A | TYR51 |
A | SER72 |
A | GLN73 |
A | ALA74 |
A | MET354 |
A | PHQ503 |
A | HOH609 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for Di-peptide PRO B 504 and PHQ B 503 |
Chain | Residue |
B | TYR51 |
B | SER72 |
B | ALA74 |
B | LEU75 |
B | PHE87 |
B | ALA330 |
B | MET354 |
B | HEM501 |
B | PHE505 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for Di-peptide PRO B 504 and PHE B 505 |
Chain | Residue |
B | LEU20 |
B | TYR51 |
B | SER72 |
B | GLN73 |
B | ALA74 |
B | LEU188 |
B | MET354 |
B | PHQ503 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for Di-peptide PRO C 504 and PHE C 505 |
Chain | Residue |
C | LEU20 |
C | TYR51 |
C | SER72 |
C | GLN73 |
C | ALA74 |
C | MET354 |
C | PHQ503 |
C | HOH637 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for Di-peptide PRO C 504 and PHQ C 503 |
Chain | Residue |
C | TYR51 |
C | SER72 |
C | ALA74 |
C | PHE87 |
C | ALA330 |
C | MET354 |
C | HEM501 |
C | PHE505 |
site_id | AD6 |
Number of Residues | 8 |
Details | binding site for Di-peptide PRO D 504 and PHE D 505 |
Chain | Residue |
D | LEU20 |
D | TYR51 |
D | SER72 |
D | GLN73 |
D | ALA74 |
D | MET354 |
D | PHQ503 |
D | HOH616 |
site_id | AD7 |
Number of Residues | 9 |
Details | binding site for Di-peptide PRO D 504 and PHQ D 503 |
Chain | Residue |
D | TYR51 |
D | SER72 |
D | ALA74 |
D | LEU75 |
D | PHE87 |
D | ALA330 |
D | MET354 |
D | HEM501 |
D | PHE505 |
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 |