MolNFT v1 · #34131 · protein
Aspartate aminotransferase mutant mabc
2D65: “Aspartate aminotransferase mutant mabc”. X-ray diffraction, 2 ligands (PLP, SO4), 5 pockets (best druggability 0.66). MolNFT v1 #34131 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2D65
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase
- EC
- 2.6.1.1
- UniProt
- P00509
- Ligands
- PLP, SO4
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 46% helix, 14% strand | P00509 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 196 | 0.66 | 0.85 | 31 | SO4, PLP |
| 2 | 86 | 0.43 | 0.79 | 18 | empty |
| 3 | 74 | 0.39 | 0.78 | 21 | empty |
| 4 | 69 | 0.31 | 0.75 | 18 | empty |
| 5 | 74 | 0.28 | 0.72 | 19 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
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 2D65 · PDBe 2D65 · UniProt P00509
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