Research workbench
Acetylornithine aminotransferase from thermus thermophilus HB8
Analyse Acetylornithine aminotransferase from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VEF
- Type
- protein
- Length
- 774 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ACETYLORNITHINE/ACETYL-lysine aminotransferase
- EC
- 2.6.1.11
- UniProt
- Q93R93
- Ligands
- PLP
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ACETYLORNITHINE/ACETYL-lysine aminotransferase (EC 2.6.1.11) | protein | 387 | 41% helix, 20% strand | Q93R93 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 642 | 0.77 | 0.82 | 69 | PLP |
| 2 | 512 | 0.75 | 0.83 | 61 | PLP |
Interfaces
1 interface between chains.
- A–B · 4831 Ų buried · 63 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1VEF · Acetylornithine aminotransferase from Thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00
- Q93R93 · AlphaFold monomer V2.0 prediction for [lysw]-aminoadipate semialdehyde transaminase… · a predicted model of the same protein · 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 Q93R93
- Elsewhere: RCSB PDB 1VEF · PDBe 1VEF · UniProt Q93R93
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