› 6xze

X-ray diffraction
1.54Å resolution

crystal structure of human carbonic anhydrase I in complex with 4-(3-(2-((2-fluorobenzyl)amino)ethyl)ureido) benzenesulfonamide

Released:
DOI: 10.2210/pdb6xze/pdb
PDB entry 6xze coloured by chain, front view.
PDB entry 6xze coloured by chain, side view.
PDB entry 6xze coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Benzylaminoethyureido-Tailed Benzenesulfonamides: Design, Synthesis, Kinetic and X-ray Investigations on Human Carbonic Anhydrases.
Ali M, Bozdag M, Farooq U, Angeli A, Carta F, Berto P, Zanotti G, Supuran CT
Int J Mol Sci 21 (2020)
PMID: 32272689

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-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

2 bound ligands:
Ligand ZN 2 x ZN
Ligand O4Z 2 x O4Z
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 62.601Å b: 71.645Å c: 121.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.214

Quick links

Citations

8 citation in other articles

4-Anilinoquinazoline-based benzenesulfonamides as nanomolar inhibitors of carbonic anhydrase isoforms I, II, IX, and XII: design, synthesis, in-vitro, and in-silico biological studies.
Nada et al. (2022)
7 more

2 mentions without citation

Benzylaminoethyureido-Tailed Benzenesulfonamides: Design, Synthesis, Kinetic and X-ray Investigations on Human Carbonic Anhydrases.
Ali et al. (2020)
1 more