MolNFT v1 · #57043 · protein
Crystal structure of lysn, alpha-aminoadipate aminotransferase (complexed with N-(5'-phosphopyridoxyl)-L-glutamate), from thermus thermophilus HB27
2ZYJ · Alpha-aminodipate aminotransferase: “Crystal structure of lysn, alpha-aminoadipate aminotransferase (complexed with…”. X-ray diffraction, 1 ligand (PGU), 6 pockets (best druggability 0.78). MolNFT v1 #57043 on GenesisL1: 3D…
- PDB
- 2ZYJ
- Type
- protein
- Length
- 794 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-aminodipate aminotransferase
- EC
- 2.6.1.39
- UniProt
- Q72LL6
- Ligands
- PGU
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alpha-aminodipate aminotransferase (EC 2.6.1.39) | protein | 397 | 49% helix, 15% strand | Q72LL6 |
Ligands and binding sites
- PGU · N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid · ligand · 2 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 114 | 0.78 | 0.97 | 33 | PGU |
| 2 | 115 | 0.78 | 0.97 | 33 | PGU |
| 3 | 156 | 0.45 | 0.76 | 25 | empty |
| 4 | 127 | 0.44 | 0.77 | 23 | empty |
| 5 | 66 | 0.43 | 0.82 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 4196 Ų buried · 75 hydrogen bonds · protein-protein
Compared structures
- 2ZYJ · Crystal structure of LysN, alpha-aminoadipate aminotransferase (complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q72LL6 · AlphaFold monomer V2.0 prediction for 2-aminoadipate transaminase (Q72LL6) · 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 Q72LL6
- Elsewhere: RCSB PDB 2ZYJ · PDBe 2ZYJ · UniProt Q72LL6
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