1J51
CRYSTAL STRUCTURE OF CYTOCHROME P450CAM MUTANT (F87W/Y96F/V247L/C334A) WITH 1,3,5-TRICHLOROBENZENE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0018683 | molecular_function | camphor 5-monooxygenase activity |
A | 0019383 | biological_process | (+)-camphor catabolic process |
A | 0020037 | molecular_function | heme binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
B | 0018683 | molecular_function | camphor 5-monooxygenase activity |
B | 0019383 | biological_process | (+)-camphor catabolic process |
B | 0020037 | molecular_function | heme binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0005506 | molecular_function | iron ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
C | 0018683 | molecular_function | camphor 5-monooxygenase activity |
C | 0019383 | biological_process | (+)-camphor catabolic process |
C | 0020037 | molecular_function | heme binding |
C | 0046872 | molecular_function | metal ion binding |
D | 0004497 | molecular_function | monooxygenase activity |
D | 0005506 | molecular_function | iron ion binding |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
D | 0018683 | molecular_function | camphor 5-monooxygenase activity |
D | 0019383 | biological_process | (+)-camphor catabolic process |
D | 0020037 | molecular_function | heme binding |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K A 1418 |
Chain | Residue |
A | GLU84 |
A | GLY93 |
A | GLU94 |
A | PHE96 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K B 2418 |
Chain | Residue |
B | GLU84 |
B | GLY93 |
B | GLU94 |
B | PHE96 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K C 3418 |
Chain | Residue |
C | GLY93 |
C | GLU94 |
C | PHE96 |
C | GLU84 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K D 4418 |
Chain | Residue |
D | GLU84 |
D | GLY93 |
D | GLU94 |
D | PHE96 |
D | HOH4475 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM A 417 |
Chain | Residue |
A | PRO100 |
A | THR101 |
A | GLN108 |
A | ARG112 |
A | LEU244 |
A | LEU245 |
A | GLY248 |
A | GLY249 |
A | THR252 |
A | ASP297 |
A | ARG299 |
A | GLN322 |
A | THR349 |
A | PHE350 |
A | GLY351 |
A | HIS355 |
A | CYS357 |
A | GLY359 |
A | ALA363 |
A | TCZ1450 |
A | HOH1452 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TCZ A 1450 |
Chain | Residue |
A | TRP87 |
A | LEU244 |
A | GLY248 |
A | THR252 |
A | VAL295 |
A | ASP297 |
A | HEM417 |
site_id | AC7 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE HEM B 417 |
Chain | Residue |
B | PRO100 |
B | THR101 |
B | GLN108 |
B | ARG112 |
B | LEU245 |
B | GLY248 |
B | THR252 |
B | VAL253 |
B | ASP297 |
B | ARG299 |
B | GLN322 |
B | THR349 |
B | PHE350 |
B | GLY351 |
B | HIS355 |
B | LEU356 |
B | CYS357 |
B | ALA363 |
B | TCZ2450 |
B | HOH2480 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TCZ B 2450 |
Chain | Residue |
B | TRP87 |
B | PHE96 |
B | LEU244 |
B | LEU247 |
B | VAL295 |
B | HEM417 |
site_id | AC9 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HEM C 417 |
Chain | Residue |
C | PRO100 |
C | THR101 |
C | GLN108 |
C | ARG112 |
C | LEU244 |
C | LEU245 |
C | GLY248 |
C | GLY249 |
C | THR252 |
C | VAL295 |
C | ASP297 |
C | ARG299 |
C | GLN322 |
C | THR349 |
C | PHE350 |
C | GLY351 |
C | HIS355 |
C | CYS357 |
C | LEU358 |
C | GLY359 |
C | TCZ3450 |
C | HOH3462 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TCZ C 3450 |
Chain | Residue |
C | HEM417 |
C | TRP87 |
C | LEU244 |
C | GLY248 |
C | THR252 |
C | VAL295 |
C | ASP297 |
site_id | BC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM D 417 |
Chain | Residue |
D | PRO100 |
D | THR101 |
D | GLN108 |
D | ARG112 |
D | LEU244 |
D | LEU245 |
D | GLY248 |
D | THR252 |
D | ASP297 |
D | ARG299 |
D | GLN322 |
D | THR349 |
D | PHE350 |
D | GLY351 |
D | HIS355 |
D | CYS357 |
D | ALA363 |
D | HOH4464 |
D | HOH4502 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGSHLCLG |
Chain | Residue | Details |
A | PHE350-GLY359 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | LEU358 | |
B | LEU358 | |
C | LEU358 | |
D | LEU358 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
A | ASP251 | |
A | THR252 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
B | ASP251 | |
B | THR252 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
C | ASP251 | |
C | THR252 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
D | ASP251 | |
D | THR252 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 133 |
Chain | Residue | Details |
A | PRO187 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | THR252 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | VAL253 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | LEU358 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
A | GLY359 | electrostatic stabiliser, hydrogen bond donor |
A | GLN360 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 133 |
Chain | Residue | Details |
B | PRO187 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | THR252 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | VAL253 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | LEU358 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
B | GLY359 | electrostatic stabiliser, hydrogen bond donor |
B | GLN360 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 133 |
Chain | Residue | Details |
C | PRO187 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | THR252 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | VAL253 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | LEU358 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
C | GLY359 | electrostatic stabiliser, hydrogen bond donor |
C | GLN360 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 133 |
Chain | Residue | Details |
D | PRO187 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | THR252 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | VAL253 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | LEU358 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
D | GLY359 | electrostatic stabiliser, hydrogen bond donor |
D | GLN360 | electrostatic stabiliser, hydrogen bond donor |