1DZ9
Putative oxo complex of P450cam from Pseudomonas putida
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 515 |
Chain | Residue |
A | GLU84 |
A | GLY93 |
A | GLU94 |
A | TYR96 |
A | HOH888 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K B 515 |
Chain | Residue |
B | HOH931 |
B | HOH929 |
B | GLU84 |
B | GLY93 |
B | GLU94 |
B | TYR96 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K K 715 |
Chain | Residue |
B | LEU14 |
B | PRO15 |
B | PRO16 |
B | VAL18 |
B | GLU20 |
B | HOH660 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM A 417 |
Chain | Residue |
A | THR101 |
A | GLN108 |
A | ARG112 |
A | LEU244 |
A | LEU245 |
A | GLY248 |
A | GLY249 |
A | THR252 |
A | ASP297 |
A | ARG299 |
A | THR349 |
A | PHE350 |
A | GLY351 |
A | HIS355 |
A | CYS357 |
A | GLY359 |
A | O502 |
A | CAM503 |
A | HOH773 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE O A 418 |
Chain | Residue |
A | HEM501 |
A | CAM503 |
A | HOH609 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CAM A 420 |
Chain | Residue |
A | PHE87 |
A | TYR96 |
A | VAL295 |
A | HEM501 |
A | O502 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TRS A 430 |
Chain | Residue |
A | PRO268 |
A | ARG271 |
A | GLN272 |
A | ILE275 |
A | PRO379 |
A | ASP380 |
A | HOH703 |
A | HOH680 |
B | GLU172 |
site_id | AC8 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM B 417 |
Chain | Residue |
B | PRO100 |
B | THR101 |
B | GLN108 |
B | ARG112 |
B | LEU244 |
B | LEU245 |
B | GLY248 |
B | GLY249 |
B | THR252 |
B | ASP297 |
B | ARG299 |
B | THR349 |
B | PHE350 |
B | GLY351 |
B | HIS355 |
B | CYS357 |
B | GLY359 |
B | HOH610 |
B | HOH893 |
B | HOH653 |
B | HOH637 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CAM B 420 |
Chain | Residue |
B | PHE87 |
B | TYR96 |
B | HOH653 |
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 | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | LEU358 | |
B | 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 | 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 |