Research workbench
Crystal structures of escherichia COLI aspartate aminotransferase reconstituted with 1-deaza-pyridoxal 5'-phosphate: internal aldimine and stable L-aspartate external aldimine
Analyse Crystal structures of escherichia COLI aspartate aminotransferase reconstituted… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QPG
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- C9QZE8
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 396 | — | C9QZE8 |
Compared structures
- 3QPG · Crystal Structures of Escherichia coli Aspartate Aminotransferase Reconstituted with… · 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 C9QZE8
- Elsewhere: RCSB PDB 3QPG · PDBe 3QPG · UniProt C9QZE8
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