› 1bqd

X-ray diffraction
2.1Å resolution

ASPARTATE AMINOTRANSFERASE P138A/P195A DOUBLE MUTANT

Released:
DOI: 10.2210/pdb1bqd/pdb
PDB entry 1bqd coloured by chain, front view.
PDB entry 1bqd coloured by chain, side view.
PDB entry 1bqd coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase.
Birolo L, Malashkevich VN, Capitani G, De Luca F, Moretta A, Jansonius JN, Marino G
Biochemistry 38 905-13 (1999)
PMID: 9893985

Function and Biology Details

Reaction catalysed: 
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132575 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 396 amino acids
Theoretical weight: 43.8 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00509 (Residues: 1-396; Coverage: 100%)
Gene names: JW0911, aspC, b0928
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT
Spacegroup: P21
Unit cell:
a: 88.49Å b: 79.88Å c: 89.68Å
α: 90° β: 119.58° γ: 90°
R-values:
R R work R free
0.205 0.204 0.24
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein.
Wu et al. (2002)
9 more