› 1heb

X-ray diffraction
2Å resolution

STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II

Released:
DOI: 10.2210/pdb1heb/pdb
PDB entry 1heb coloured by chain, front view.
PDB entry 1heb coloured by chain, side view.
PDB entry 1heb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural consequences of hydrophilic amino acid substitutions in the hydrophobic pocket of human carbonic anhydrase II.
Nair SK, Christianson DW
Biochemistry 32 4506-14 (1993)
PMID: 8485129

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: 29.31 KDa
Source organism: Homo sapiens
Expression system: Not provided
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 HG 1 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 42.7Å b: 41.7Å c: 73Å
α: 90° β: 104.6° γ: 90°
R-values:
R R work R free
0.18 not available not available
Expression system: Not provided

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

2 mentions without citation

Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view.
Lu et al. (2016)
1 more