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Structure of human protoporphyrinogen IX OXIDASE(R59Q)
Analyse Structure of human protoporphyrinogen IX OXIDASE(R59Q) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IVO
- Type
- protein
- Length
- 464 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protoporphyrinogen oxidase
- EC
- 1.3.3.4
- UniProt
- P50336
- Ligands
- ACJ, FAD
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Protoporphyrinogen oxidase (EC 1.3.3.4) | protein | 464 | 39% helix, 21% strand | P50336 |
Ligands and binding sites
- ACJ · 5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid · ligand · chains B
- FAD · Flavin-adenine dinucleotide · ligand · chains B
- GOL · Glycerol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1006 | 0.82 | 0.83 | 101 | ACJ, FAD |
| 2 | 143 | 0.43 | 0.75 | 20 | empty |
| 3 | 86 | 0.42 | 0.79 | 24 | empty |
| 4 | 57 | 0.38 | 0.80 | 13 | empty |
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P50336
- Elsewhere: RCSB PDB 4IVO · PDBe 4IVO · UniProt P50336
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