Research workbench
Mechanism of inactivation of E. COLI aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-furancarboxylic acid (S-adfa) pH 8.0
Analyse Mechanism of inactivation of E. COLI aspartate aminotransferase by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PAA
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D3H0F7
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 396 | — | D3H0F7 |
Compared structures
- 3PAA · Mechanism of inactivation of E. coli aspartate aminotransferase by… · the same entry in another collection · 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 D3H0F7
- Elsewhere: RCSB PDB 3PAA · PDBe 3PAA · UniProt D3H0F7
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