MolNFT v1 · #815 · protein
Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal-5'-phosphate binding lysine residue
1AIB: “Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the…”. X-ray diffraction, 2 ligands (PMP, AKG), 10 pockets (best druggability 0.72). MolNFT v1 #815 on GenesisL1: 3D structure, binding sites…
- PDB
- 1AIB
- 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
- PMP, AKG
- Pockets
- 10 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 46% helix, 14% strand | P00509 |
Ligands and binding sites
- PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- AKG · 2-oxoglutaric 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 561 | 0.72 | 0.81 | 73 | PMP, AKG |
| 2 | 555 | 0.71 | 0.80 | 73 | PMP, AKG |
| 3 | 57 | 0.35 | 0.78 | 22 | empty |
| 4 | 53 | 0.35 | 0.78 | 15 | empty |
| 5 | 61 | 0.34 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 3148 Ų buried · 59 hydrogen bonds · protein-protein
Compared structures
- 1AIB · Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking… · 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 1AIB · PDBe 1AIB · UniProt P00509
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