› 4qsj

X-ray diffraction
1.7Å resolution

Crystal structure of human carbonic anhydrase isozyme XIII with 2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)thio]acetyl}benzenesulfonamide

Released:
DOI: 10.2210/pdb4qsj/pdb
PDB entry 4qsj coloured by chain, front view.
PDB entry 4qsj coloured by chain, side view.
PDB entry 4qsj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Intrinsic Thermodynamics and Structure Correlation of Benzenesulfonamides with a Pyrimidine Moiety Binding to Carbonic Anhydrases I, II, VII, XII, and XIII.
Kišonaitė M, Zubrienė A, Capkauskaitė E, Smirnov A, Smirnovienė J, Kairys V, Michailovienė V, Manakova E, Gražulis S, Matulis D
PLoS One 9 e114106 (2014)
PMID: 25493428

Function and Biology Details

Reaction catalysed: 
H(2)CO(3) = CO(2) + 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-185360 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 13 Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 29.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8N1Q1 (Residues: 1-262; Coverage: 100%)
Gene name: CA13
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

7 bound ligands:
Ligand ZN 2 x ZN
Ligand EWW 2 x EWW
Ligand PEG 2 x PEG
Ligand DMS 1 x DMS
Ligand CIT 2 x CIT
Ligand EDO 2 x EDO
Ligand NI 1 x NI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P212121
Unit cell:
a: 56.66Å b: 57.78Å c: 160.077Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.164 0.204
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Reconsidering anion inhibitors in the general context of drug design studies of modulators of activity of the classical enzyme carbonic anhydrase.
Nocentini et al. (2021)
1 more

1 mention without citation

Intrinsic Thermodynamics and Structure Correlation of Benzenesulfonamides with a Pyrimidine Moiety Binding to Carbonic Anhydrases I, II, VII, XII, and XIII.
Kišonaitė et al. (2014)