3I6D
Crystal structure of PPO from bacillus subtilis with AF
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004729 | molecular_function | oxygen-dependent protoporphyrinogen oxidase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
A | 0006783 | biological_process | heme biosynthetic process |
A | 0016020 | cellular_component | membrane |
A | 0016117 | biological_process | carotenoid biosynthetic process |
A | 0016166 | molecular_function | phytoene dehydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
B | 0004729 | molecular_function | oxygen-dependent protoporphyrinogen oxidase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005886 | cellular_component | plasma membrane |
B | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
B | 0006783 | biological_process | heme biosynthetic process |
B | 0016020 | cellular_component | membrane |
B | 0016117 | biological_process | carotenoid biosynthetic process |
B | 0016166 | molecular_function | phytoene dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE FAD A 600 |
Chain | Residue |
A | GLY12 |
A | LYS49 |
A | GLY63 |
A | PRO64 |
A | ASP65 |
A | SER66 |
A | THR254 |
A | LYS255 |
A | VAL256 |
A | TRP409 |
A | SER412 |
A | GLY13 |
A | ALA443 |
A | VAL448 |
A | ILE450 |
A | CYS453 |
A | ACJ471 |
A | GLY14 |
A | ILE15 |
A | THR16 |
A | VAL40 |
A | GLU41 |
A | ALA42 |
A | GLY48 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACJ A 471 |
Chain | Residue |
A | LEU68 |
A | LYS71 |
A | ILE176 |
A | MET413 |
A | FAD600 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 A 472 |
Chain | Residue |
A | SER144 |
A | LYS145 |
A | THR146 |
A | GLN150 |
A | ARG158 |
A | ARG159 |
site_id | AC4 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE FAD B 700 |
Chain | Residue |
B | GLY12 |
B | GLY14 |
B | ILE15 |
B | THR16 |
B | GLU41 |
B | ALA42 |
B | GLY48 |
B | LYS49 |
B | GLY63 |
B | PRO64 |
B | ASP65 |
B | SER66 |
B | LYS255 |
B | VAL256 |
B | THR284 |
B | ALA285 |
B | ALA289 |
B | TRP409 |
B | SER412 |
B | GLY442 |
B | ALA443 |
B | VAL448 |
B | ILE450 |
B | CYS453 |
B | ACJ471 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACJ B 471 |
Chain | Residue |
B | LYS71 |
B | ILE176 |
B | TYR177 |
B | MET413 |
B | VAL448 |
B | FAD700 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 B 472 |
Chain | Residue |
B | SER144 |
B | LYS145 |
B | THR146 |
B | GLN150 |
B | ARG158 |
B | ARG159 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19944166 |
Chain | Residue | Details |
B | LYS49 | |
B | GLY63 | |
B | TRP409 | |
B | VAL448 | |
A | GLY12 | |
A | GLU41 | |
A | LYS49 | |
A | GLY63 | |
A | TRP409 | |
A | VAL448 | |
B | GLY12 | |
B | GLU41 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P56601 |
Chain | Residue | Details |
A | VAL256 | |
B | VAL256 |