› 4hu1

X-ray diffraction
1.95Å resolution

Crystal structure of human carbonic anhydrase isozyme XIII with the inhibitor.

Released:
DOI: 10.2210/pdb4hu1/pdb
PDB entry 4hu1 coloured by chain, front view.
PDB entry 4hu1 coloured by chain, side view.
PDB entry 4hu1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
4-Substituted-2,3,5,6-tetrafluorobenzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, XII, and XIII.
Dudutienė V, Zubrienė A, Smirnov A, Gylytė J, Timm D, Manakova E, Gražulis S, Matulis D
Bioorg Med Chem 21 2093-106 (2013)
PMID: 23394791

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

4 bound ligands:
Ligand ZN 2 x ZN
Ligand V13 2 x V13
Ligand EDO 7 x EDO
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 56.27Å b: 57.386Å c: 159.552Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.169 0.235
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Thermodynamic, kinetic, and structural parameterization of human carbonic anhydrase interactions toward enhanced inhibitor design.
Linkuvienė et al. (2018)
29 other articles

1 mention without citation

Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding.
Smirnov et al. (2018)