MolNFT v1 · #137252 · protein
Crystal structure of acetylornithine aminotransferase from elizabethkingia anophelis
5VIU: “Crystal structure of acetylornithine aminotransferase from elizabethkingia anophelis”. X-ray diffraction, 6 pockets (best druggability 0.84). MolNFT v1 #137252 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5VIU
- Type
- protein
- Length
- 784 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylornithine aminotransferase
- EC
- 2.6.1.11
- UniProt
- A0A077E919
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylornithine aminotransferase (EC 2.6.1.11) | protein | 401 | 40% helix, 20% strand | A0A077E919 |
| B | Acetylornithine aminotransferase (EC 2.6.1.11) | protein | 383 | 43% helix, 21% strand | A0A077E919 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains A, B
- CIT · Citric acid · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1100 | 0.84 | 0.85 | 109 | CIT |
| 2 | 65 | 0.49 | 0.84 | 14 | empty |
| 3 | 90 | 0.45 | 0.80 | 14 | empty |
| 4 | 78 | 0.38 | 0.77 | 15 | empty |
| 5 | 52 | 0.35 | 0.79 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 4209 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 5VIU · Crystal Structure of Acetylornithine Aminotransferase from Elizabethkingia anophelis · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A077E919
- Elsewhere: RCSB PDB 5VIU · PDBe 5VIU · UniProt A0A077E919
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