› 6rvk

X-ray diffraction
1.58Å resolution

Crystal structure of hCA II in complex with Urea, N-(1,3-dihydro-1-hydroxy-2,1-benzoxaborol-6-yl)-N'-(phenylmethyl)-

Released:
DOI: 10.2210/pdb6rvk/pdb
PDB entry 6rvk coloured by chain, front view.
PDB entry 6rvk coloured by chain, side view.
PDB entry 6rvk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Exploring benzoxaborole derivatives as carbonic anhydrase inhibitors: a structural and computational analysis reveals their conformational variability as a tool to increase enzyme selectivity.
Langella E, Alterio V, D'Ambrosio K, Cadoni R, Winum JY, Supuran CT, Monti SM, De Simone G, Di Fiore A
J Enzyme Inhib Med Chem 34 1498-1505 (2019)
PMID: 31423863

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: 262 amino acids
Theoretical weight: 29.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00918 (Residues: 1-260; Coverage: 100%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand R29 1 x R29
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 42.35Å b: 41.36Å c: 72.17Å
α: 90° β: 104.23° γ: 90°
R-values:
R R work R free
0.169 0.169 0.197
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Carbonic Anhydrase Inhibitors Targeting Metabolism and Tumor Microenvironment.
Angeli et al. (2020)
2 more

1 mention without citation

Exploring benzoxaborole derivatives as carbonic anhydrase inhibitors: a structural and computational analysis reveals their conformational variability as a tool to increase enzyme selectivity.
Langella et al. (2019)