MolNFT v1 · #49019 · protein
Structural studies reveal the inactivation of E. COLI L-aspartate aminotransferase by (S)-4,5-dihydro-2-thiophenecarboxylic acid (sadta) via two mechanisms (at pH 7.5)
2QB3: “Structural studies reveal the inactivation of E. COLI L-aspartate aminotransferase by…”. X-ray diffraction. MolNFT v1 #49019 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2QB3
- Type
- protein
- Length
- 383 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00509
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 383 | — | P00509 |
Compared structures
- 2QB3 · Structural Studies Reveal the Inactivation of E. coli L-Aspartate Aminotransferase by… · 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 0.99
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 2QB3 · PDBe 2QB3 · UniProt P00509
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