1SEZ
Crystal Structure of 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 | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0009507 | cellular_component | chloroplast |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0004729 | molecular_function | oxygen-dependent protoporphyrinogen oxidase activity |
| B | 0005739 | cellular_component | mitochondrion |
| 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 | 0009507 | cellular_component | chloroplast |
| B | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD A 600 |
| Chain | Residue |
| A | ILE19 |
| A | LYS51 |
| A | GLY65 |
| A | ALA66 |
| A | ASN67 |
| A | THR68 |
| A | ARG263 |
| A | VAL264 |
| A | ALA304 |
| A | ASP308 |
| A | VAL336 |
| A | GLY20 |
| A | ALA438 |
| A | PHE439 |
| A | ASN468 |
| A | SER474 |
| A | VAL475 |
| A | OMN601 |
| A | HOH608 |
| A | GLY22 |
| A | VAL23 |
| A | SER24 |
| A | PHE42 |
| A | GLU43 |
| A | ALA44 |
| A | GLY50 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD B 610 |
| Chain | Residue |
| B | GLY20 |
| B | GLY22 |
| B | VAL23 |
| B | SER24 |
| B | PHE42 |
| B | GLU43 |
| B | ALA44 |
| B | GLY50 |
| B | LYS51 |
| B | GLY65 |
| B | ALA66 |
| B | ASN67 |
| B | THR68 |
| B | ARG263 |
| B | VAL264 |
| B | ALA304 |
| B | ASP308 |
| B | ALA438 |
| B | PHE439 |
| B | ASN468 |
| B | SER474 |
| B | VAL475 |
| B | OMN604 |
| B | HOH618 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE OMN A 601 |
| Chain | Residue |
| A | ARG98 |
| A | ALA174 |
| A | GLY175 |
| A | CYS177 |
| A | GLY178 |
| A | LEU334 |
| A | GLY354 |
| A | LEU356 |
| A | LEU369 |
| A | GLY370 |
| A | THR371 |
| A | LEU372 |
| A | PHE392 |
| A | FAD600 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE TON A 603 |
| Chain | Residue |
| A | LEU109 |
| A | LEU168 |
| A | PHE172 |
| A | LEU356 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE OMN B 604 |
| Chain | Residue |
| B | ARG98 |
| B | ALA174 |
| B | GLY175 |
| B | CYS177 |
| B | GLY178 |
| B | LEU334 |
| B | GLY354 |
| B | VAL355 |
| B | LEU356 |
| B | LEU369 |
| B | GLY370 |
| B | THR371 |
| B | PHE392 |
| B | TON605 |
| B | FAD610 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TON B 605 |
| Chain | Residue |
| B | LEU109 |
| B | LEU168 |
| B | PHE172 |
| B | PHE190 |
| B | LEU356 |
| B | OMN604 |
| B | HOH621 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15057273 |
| Chain | Residue | Details |
| B | GLU43 | |
| B | LYS51 | |
| B | GLY65 | |
| B | VAL264 | |
| B | LEU473 | |
| A | GLY20 | |
| A | GLU43 | |
| A | LYS51 | |
| A | GLY65 | |
| A | VAL264 | |
| A | LEU473 | |
| B | GLY20 |
