› 1ugg

X-ray diffraction
2.2Å resolution

HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)-ORTHORHOMBIC FORM

Released:
DOI: 10.2210/pdb1ugg/pdb
PDB entry 1ugg coloured by chain, front view.
PDB entry 1ugg coloured by chain, side view.
PDB entry 1ugg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis.
Scolnick LR, Christianson DW
Biochemistry 35 16429-34 (1996)
PMID: 8987974

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: 258 amino acids
Theoretical weight: 29.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00918 (Residues: 3-260; Coverage: 99%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 42.5Å b: 72.7Å c: 75.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.282
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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

1 mention without citation

Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase II.
Boone et al. (2015)