› 4kv0

X-ray diffraction
1.55Å resolution

Crystal structure of human carbonic anhydrase II in complex with the 5-(3-tosylureido)pyridine-2-sulfonamide inhibitor

Released:
DOI: 10.2210/pdb4kv0/pdb
PDB entry 4kv0 coloured by chain, front view.
PDB entry 4kv0 coloured by chain, side view.
PDB entry 4kv0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Combining the tail and the ring approaches for obtaining potent and isoform-selective carbonic anhydrase inhibitors: solution and X-ray crystallographic studies.
Bozdag M, Ferraroni M, Nuti E, Vullo D, Rossello A, Carta F, Scozzafava A, Supuran CT
Bioorg Med Chem 22 334-40 (2014)
PMID: 24300919

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 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: 257 amino acids
Theoretical weight: 28.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P00918 (Residues: 4-260; Coverage: 99%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand GOL 1 x GOL
Ligand BME 1 x BME
Ligand MB7 1 x MB7
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: P21
Unit cell:
a: 42.249Å b: 41.283Å c: 72.055Å
α: 90° β: 104.28° γ: 90°
R-values:
R R work R free
0.159 0.158 0.179
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

Advances in structure-based drug discovery of carbonic anhydrase inhibitors.
Supuran CT. (2017)
8 more

1 mention without citation

Structural analyses of 4-phosphate adaptor protein 2 yield mechanistic insights into sphingolipid recognition by the glycolipid transfer protein family.
Ochoa-Lizarralde et al. (2018)