› 1rzd

X-ray diffraction
1.9Å resolution

X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES

Released:
DOI: 10.2210/pdb1rzd/pdb
PDB entry 1rzd coloured by chain, front view.
PDB entry 1rzd coloured by chain, side view.
PDB entry 1rzd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
X-ray analysis of metal-substituted human carbonic anhydrase II derivatives.
Håkansson K, Wehnert A, Liljas A
Acta Crystallogr D Biol Crystallogr 50 93-100 (1994)
PMID: 15299481

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: 259 amino acids
Theoretical weight: 29.16 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00918 (Residues: 2-260; Coverage: 100%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

2 bound ligands:
Ligand MN 1 x MN
Ligand SO4 1 x SO4
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
0.148 not available not available
Expression system: Not provided

Quick links

Citations

5 review citations

Structural annotation of human carbonic anhydrases.
Aggarwal et al. (2013)
4 more

1 mention without citation

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