MolNFT v1 · #47199 · protein
Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (TM1785) from thermotoga maritima at 1.40 a resolution
2ORD: “Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (TM1785) from thermotoga maritima…”. X-ray diffraction, 1 ligand (PLP), 2 pockets (best druggability 0.79). MolNFT v1 #47199 on GenesisL1: 3D structure…
- PDB
- 2ORD
- Type
- protein
- Length
- 786 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylornithine aminotransferase
- EC
- 2.6.1.11
- UniProt
- Q9X2A5
- Ligands
- PLP
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acetylornithine aminotransferase (EC 2.6.1.11) | protein | 393 | 41% helix, 21% strand | Q9X2A5 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 17 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 | 484 | 0.79 | 0.86 | 55 | PLP, GOL |
| 2 | 442 | 0.76 | 0.85 | 55 | PLP, GOL |
Interfaces
1 interface between chains.
- A–B · 5260 Ų buried · 76 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 2ORD · Crystal structure of Acetylornithine aminotransferase (EC 2.6.1.11) (ACOAT) (TM1785) from… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X2A5 · AlphaFold monomer V2.0 prediction for acetylornithine aminotransferase (Q9X2A5) · a predicted model of the same protein · chain B 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 Q9X2A5
- Elsewhere: RCSB PDB 2ORD · PDBe 2ORD · UniProt Q9X2A5
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