Research workbench
Coproporphyrinogen III oxidase from leishmania major
Analyse Coproporphyrinogen III oxidase from leishmania major in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QT8
- Type
- protein
- Length
- 606 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coproporphyrinogen III oxidase
- EC
- 1.3.3.3
- UniProt
- P84155
- Pockets
- 8 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coproporphyrinogen III oxidase (EC 1.3.3.3) | protein | 302 | 45% helix, 28% strand | P84155 |
| B | Coproporphyrinogen III oxidase (EC 1.3.3.3) | protein | 304 | 46% helix, 28% strand | P84155 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 782 | 0.84 | 0.87 | 67 | ACT |
| 2 | 789 | 0.83 | 0.86 | 62 | ACT |
| 3 | 123 | 0.40 | 0.75 | 20 | empty |
| 4 | 78 | 0.38 | 0.77 | 19 | empty |
| 5 | 91 | 0.36 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1350 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2QT8 · Coproporphyrinogen III oxidase from Leishmania major · the same entry in another collection · chain A against A, TM-score 1.00
- P84155 · AlphaFold monomer V2.0 prediction for oxygen-dependent coproporphyrinogen-III oxidase… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P84155
- Elsewhere: RCSB PDB 2QT8 · PDBe 2QT8 · UniProt P84155
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