› 2geh

X-ray diffraction
2Å resolution

N-Hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors

Released:
DOI: 10.2210/pdb2geh/pdb
PDB entry 2geh coloured by chain, front view.
PDB entry 2geh coloured by chain, side view.
PDB entry 2geh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
N-hydroxyurea--a versatile zinc binding function in the design of metalloenzyme inhibitors.
Temperini C, Innocenti A, Scozzafava A, Supuran CT
Bioorg Med Chem Lett 16 4316-20 (2006)
PMID: 16759856

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: 29.29 KDa
Source organism: Homo sapiens
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

3 bound ligands:
Ligand ZN 1 x ZN
Ligand HG 2 x HG
Ligand NHY 1 x NHY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: P21
Unit cell:
a: 42.201Å b: 41.453Å c: 72.268Å
α: 90° β: 104.4° γ: 90°
R-values:
R R work R free
0.207 0.199 0.229

Quick links

Citations

4 review citations

Ribonucleotide reductase and cancer: biological mechanisms and targeted therapies.
Aye et al. (2015)
3 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)