MolNFT v1 · #26861 · protein
Crystal structure of E.COLI aspat complexed with N-phosphopyridoxyl-D- glutamic acid
1X2A · Aspartate aminotransferase: “Crystal structure of E.COLI aspat complexed with N-phosphopyridoxyl-D- glutamic acid”. X-ray diffraction, 1 ligand (PDG), 10 pockets (best druggability 0.80). MolNFT v1 #26861 on GenesisL1: 3D structure…
- PDB
- 1X2A
- Type
- protein
- Length
- 792 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase
- EC
- 2.6.1.1
- UniProt
- P00509
- Ligands
- PDG
- Pockets
- 10 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 48% helix, 14% strand | P00509 |
Ligands and binding sites
- PDG · N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-D-glutamic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.80 | 0.97 | 30 | PDG |
| 2 | 138 | 0.79 | 0.97 | 32 | PDG |
| 3 | 288 | 0.55 | 0.76 | 49 | empty |
| 4 | 265 | 0.54 | 0.76 | 45 | empty |
| 5 | 91 | 0.40 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 3310 Ų buried · 67 hydrogen bonds · protein-protein
Compared structures
- 1X2A · Crystal Structure of e.coli AspAT complexed with N-phosphopyridoxyl-D-glutamic acid · the same entry in another collection · chain A against A, TM-score 1.00
- P00509 · AlphaFold monomer V2.0 prediction for aspartate aminotransferase (P00509) · 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 P00509
- Elsewhere: RCSB PDB 1X2A · PDBe 1X2A · UniProt P00509
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