› 6i0l

X-ray diffraction
1.4Å resolution

Crystal structure of human carbonic anhydrase I in complex with the 1-[4-chloro-3-(trifluoromethyl)phenyl]-3-[2-(4-sulfamoylphenyl)ethyl]urea inhibitor

Released:
DOI: 10.2210/pdb6i0l/pdb
Model geometry
Fit model/data
PDB entry 6i0l coloured by chain, front view.
PDB entry 6i0l coloured by chain, side view.
PDB entry 6i0l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Carbonic anhydrase inhibitors based on sorafenib scaffold: Design, synthesis, crystallographic investigation and effects on primary breast cancer cells.
Bozdag M, Ferraroni M, Ward C, Carta F, Bua S, Angeli A, Langdon SP, Kunkler IH, Al-Tamimi AS, Supuran CT
Eur J Med Chem 182 111600 (2019)
PMID: 31419777

Function and Biology Details

Reactions catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Urea = cyanamide + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133680 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 261 amino acids
Theoretical weight: 28.91 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00915 (Residues: 1-261; Coverage: 100%)
Gene name: CA1
Sequence domains: Eukaryotic-type carbonic anhydrase

Ligands and Environments

4 bound ligands:
Ligand ZN 2 x ZN
Ligand GZH 2 x GZH
Ligand GOL 3 x GOL
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: P212121
Unit cell:
a: 62.461Å b: 70.453Å c: 121.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.237

Quick links

Citations

3 review citations

Perspectives on the Classical Enzyme Carbonic Anhydrase and the Search for Inhibitors.
Jonsson et al. (2020)
2 more

2 mentions without citation

Cytotoxic effect, enzyme inhibition, and in silico studies of some novel N-substituted sulfonyl amides incorporating 1,3,4-oxadiazol structural motif.
Güleç et al. (2022)
1 more