3NKS
Structure of human protoporphyrinogen IX oxidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004729 | molecular_function | oxygen-dependent protoporphyrinogen oxidase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0006784 | biological_process | heme A biosynthetic process |
| A | 0006785 | biological_process | heme B biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031966 | cellular_component | mitochondrial membrane |
| A | 0048034 | biological_process | heme O biosynthetic process |
| A | 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 A 478 |
| Chain | Residue |
| A | ARG97 |
| A | LEU344 |
| A | GLY345 |
| A | VAL347 |
| A | MET368 |
| A | ILE419 |
| A | FAD479 |
| A | HOH530 |
| A | HOH536 |
| A | ARG168 |
| A | GLY169 |
| A | VAL170 |
| A | ALA172 |
| A | PHE331 |
| A | GLY332 |
| A | HIS333 |
| A | LEU334 |
| site_id | AC2 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD A 479 |
| Chain | Residue |
| A | GLY9 |
| A | GLY11 |
| A | ILE12 |
| A | SER13 |
| A | VAL33 |
| A | GLU34 |
| A | SER35 |
| A | GLY41 |
| A | TRP42 |
| A | LEU56 |
| A | GLY57 |
| A | PRO58 |
| A | ARG59 |
| A | GLY60 |
| A | PRO256 |
| A | VAL257 |
| A | ALA285 |
| A | ILE286 |
| A | VAL316 |
| A | GLY448 |
| A | ALA449 |
| A | VAL454 |
| A | ALA455 |
| A | VAL456 |
| A | CYS459 |
| A | ACJ478 |
| A | HOH480 |
| A | HOH481 |
| A | HOH484 |
| A | HOH497 |
| A | HOH510 |
| A | HOH531 |
| A | HOH533 |
| A | HOH535 |
| A | HOH541 |
| A | HOH615 |
| A | HOH625 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 968 |
| Chain | Residue |
| A | GLY425 |
| A | GLN428 |
| A | LYS429 |
| A | SER432 |
| A | HOH729 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 969 |
| Chain | Residue |
| A | ALA214 |
| A | TRP427 |
| A | ARG434 |
| A | GLU452 |
| A | HOH492 |
| A | HOH548 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21048046 |
| Chain | Residue | Details |
| A | GLY9 | |
| A | GLU34 | |
| A | TRP42 | |
| A | GLY57 | |
| A | VAL257 | |
| A | ALA449 | |
| A | VAL454 |
