4IVM
Structure of human protoporphyrinogen IX oxidase(R59G)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0004729 | molecular_function | oxygen-dependent protoporphyrinogen oxidase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005758 | cellular_component | mitochondrial intermembrane space |
| B | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| B | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| B | 0006783 | biological_process | heme biosynthetic process |
| B | 0006784 | biological_process | heme A biosynthetic process |
| B | 0006785 | biological_process | heme B biosynthetic process |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0031966 | cellular_component | mitochondrial membrane |
| B | 0046501 | biological_process | protoporphyrinogen IX metabolic process |
| B | 0048034 | biological_process | heme O biosynthetic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ACJ B 501 |
| Chain | Residue |
| B | ARG97 |
| B | LEU344 |
| B | GLY345 |
| B | ILE346 |
| B | VAL347 |
| B | MET368 |
| B | ILE419 |
| B | FAD502 |
| B | HOH602 |
| B | ARG168 |
| B | GLY169 |
| B | VAL170 |
| B | ALA172 |
| B | PHE331 |
| B | GLY332 |
| B | HIS333 |
| B | LEU334 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD B 502 |
| Chain | Residue |
| B | GLY9 |
| B | GLY11 |
| B | ILE12 |
| B | SER13 |
| B | VAL33 |
| B | GLU34 |
| B | SER35 |
| B | GLY41 |
| B | TRP42 |
| B | LEU56 |
| B | GLY57 |
| B | PRO58 |
| B | GLY60 |
| B | PRO256 |
| B | VAL257 |
| B | ALA285 |
| B | ILE286 |
| B | VAL316 |
| B | GLY448 |
| B | ALA449 |
| B | VAL454 |
| B | ALA455 |
| B | VAL456 |
| B | CYS459 |
| B | ACJ501 |
| B | HOH611 |
| B | HOH613 |
| B | HOH640 |
| B | HOH641 |
| B | HOH643 |
| B | HOH647 |
| B | HOH662 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | GLY425 |
| B | GLN428 |
| B | LYS429 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 504 |
| Chain | Residue |
| B | SER182 |
| B | ALA214 |
| B | ARG434 |
| B | GLU452 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21048046","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
