MolNFT v1 · #34132 · protein
Aspartate aminotransferase mutant mab
2D66: “Aspartate aminotransferase mutant mab”. X-ray diffraction, 2 ligands (PLP, SO4), 7 pockets (best druggability 0.65). MolNFT v1 #34132 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2D66
- 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
- 7 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 48% helix, 14% strand | P00509 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.65 | 0.85 | 31 | SO4, PLP |
| 2 | 124 | 0.45 | 0.77 | 26 | empty |
| 3 | 80 | 0.37 | 0.77 | 21 | empty |
| 4 | 64 | 0.36 | 0.78 | 15 | empty |
| 5 | 61 | 0.29 | 0.74 | 16 | 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 2D66 · PDBe 2D66 · UniProt P00509
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