› 1ct9

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1ct9/pdb
PDB entry 1ct9 coloured by chain, front view.
PDB entry 1ct9 coloured by chain, side view.
PDB entry 1ct9 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product.
Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I
Biochemistry 38 16146-57 (1999)
PMID: 10587437

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149525 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Asparagine synthetase B [glutamine-hydrolyzing] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 553 amino acids
Theoretical weight: 62.58 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P22106 (Residues: 2-554; Coverage: 100%)
Gene names: JW0660, asnB, b0674
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand IUM 16 x IUM
Ligand CL 4 x CL
Ligand AMP 4 x AMP
Ligand GLN 4 x GLN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 99.93Å b: 127.1Å c: 204.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.297
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Channeling of substrates and intermediates in enzyme-catalyzed reactions.
Huang et al. (2001)
13 more

25 mentions without citation

Asparagine synthetase: Function, structure, and role in disease.
Lomelino et al. (2017)
24 more