› 1csh

X-ray diffraction
1.65Å resolution

A very short hydrogen bond provides only moderate stabilization of an enzyme: inhibitor complex of citrate synthase

Released:
DOI: 10.2210/pdb1csh/pdb
PDB entry 1csh coloured by chain, front view.
PDB entry 1csh coloured by chain, side view.
PDB entry 1csh coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
A very short hydrogen bond provides only moderate stabilization of an enzyme-inhibitor complex of citrate synthase.
Usher KC, Remington SJ, Martin DP, Drueckhammer DG
Biochemistry 33 7753-9 (1994)
PMID: 8011640

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA
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-149859 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Citrate synthase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 435 amino acids
Theoretical weight: 48.17 KDa
Source organism: Gallus gallus
Expression system: Not provided
UniProt:
  • Canonical: P23007 (Residues: 3-433; Coverage: 100%)
Gene name: CS
Sequence domains: Citrate synthase, C-terminal domain
Structure domains:

Ligands and Environments


Cofactor: Ligand AMX 1 x AMX
1 bound ligand:
Ligand OAA 1 x OAA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 104.4Å b: 78.5Å c: 58.5Å
α: 90° β: 78.9° γ: 90°
R-values:
R R work R free
0.164 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

"Strong" hydrogen bonds in chemistry and biology.
Perrin et al. (1997)
3 more

15 mentions without citation

Low barrier hydrogen bonds in protein structure and function.
Kemp et al. (2021)
14 more