› 1lg6

X-ray diffraction
2.2Å resolution

Crystal Structure Analysis of HCA II Mutant T199P in Complex with Thiocyanate

Released:
DOI: 10.2210/pdb1lg6/pdb
PDB entry 1lg6 coloured by chain, front view.
PDB entry 1lg6 coloured by chain, side view.
PDB entry 1lg6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Organization of an efficient carbonic anhydrase: implications for the mechanism based on structure-function studies of a T199P/C206S mutant.
Huang S, Sjöblom B, Sauer-Eriksson AE, Jonsson BH
Biochemistry 41 7628-35 (2002)
PMID: 12056894

Function and Biology Details

Reactions catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Urea = cyanamide + 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-133681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 2 Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 29.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00918 (Residues: 1-260; Coverage: 100%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: C2
Unit cell:
a: 66.516Å b: 51.315Å c: 81.003Å
α: 90° β: 107.57° γ: 90°
R-values:
R R work R free
0.201 0.197 0.252
Expression system: Escherichia coli

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Citations

2 review citations

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