› 1flj

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III

Released:
DOI: 10.2210/pdb1flj/pdb
PDB entry 1flj coloured by chain, front view.
PDB entry 1flj coloured by chain, side view.
PDB entry 1flj coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of S-glutathiolated carbonic anhydrase III.
Mallis RJ, Poland BW, Chatterjee TK, Fisher RA, Darmawan S, Honzatko RB, Thomas JA
FEBS Lett 482 237-41 (2000)
PMID: 11024467

Function and Biology Details

Reaction catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146857 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 3 Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 29.37 KDa
Source organism: Rattus norvegicus
UniProt:
  • Canonical: P14141 (Residues: 2-260; Coverage: 100%)
Gene name: Ca3
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand GSH 2 x GSH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P21
Unit cell:
a: 41.25Å b: 44.73Å c: 66.91Å
α: 90° β: 99.73° γ: 90°
R-values:
R R work R free
0.155 0.155 0.213

Quick links

Citations

16 review citations

S-glutathionylation in protein redox regulation.
Dalle-Donne et al. (2007)
15 more

11 mentions without citation

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
Krishnamurthy et al. (2008)
10 more