Research workbench
2.8-ångströms-resolution crystal structure of an active-site mutant of aspartate aminotransferase from escherichia COLI
Analyse 2.8-ångströms-resolution crystal structure of an active-site mutant of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AAT
- 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
- PMP, SO4
- Pockets
- 8 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 396 | 36% helix, 10% strand | P00509 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.71 | 0.98 | 16 | empty |
| 2 | 328 | 0.63 | 0.79 | 50 | SO4, PMP |
| 3 | 84 | 0.53 | 0.85 | 23 | empty |
| 4 | 90 | 0.41 | 0.78 | 22 | empty |
| 5 | 96 | 0.35 | 0.74 | 17 | empty |
Compared structures
- 2AAT · 2.8-ångströms-resolution crystal structure of an active-site mutant of aspartate… · 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 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 P00509
- Elsewhere: RCSB PDB 2AAT · PDBe 2AAT · UniProt P00509
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