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
- 1WKG
- 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
- POI
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ACETYLORNITHINE/ACETYL-lysine aminotransferase (EC 2.6.1.11) | protein | 387 | 41% helix, 19% strand | Q93R93 |
Ligands and binding sites
- POI · N~2~-acetyl-N~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-ornithine · 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 | 575 | 0.79 | 0.85 | 63 | POI |
| 2 | 581 | 0.77 | 0.83 | 67 | POI |
Interfaces
1 interface between chains.
- A–B · 4700 Ų buried · 58 hydrogen bonds · protein-protein
Compared structures
- 1WKG · Acetylornithine aminotransferase from thermus thermophilus HB8 · the same entry in another collection · chain B against B, 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 1WKG · PDBe 1WKG · UniProt Q93R93
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.