› 6rs5

X-ray diffraction
1.07Å resolution

Human Carbonic Anhydrase II in complex with fluorinated benzenesulfonamide

Released:
DOI: 10.2210/pdb6rs5/pdb
PDB entry 6rs5 coloured by chain, front view.
PDB entry 6rs5 coloured by chain, side view.
PDB entry 6rs5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The Influence of Varying Fluorination Patterns on the Thermodynamics and Kinetics of Benzenesulfonamide Binding to Human Carbonic Anhydrase II.
Glöckner S, Ngo K, Wagner B, Heine A, Klebe G
OpenAccess logo Biomolecules 10 (2020)
PMID: 32230853

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: 265 amino acids
Theoretical weight: 29.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00918 (Residues: 1-260; Coverage: 100%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase

Ligands and Environments

6 bound ligands:
Ligand ZN 1 x ZN
Ligand HG 1 x HG
Ligand BE7 1 x BE7
Ligand BGC 1 x BGC
Ligand KGK 2 x KGK
Ligand GLC 1 x GLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21
Unit cell:
a: 42.381Å b: 41.533Å c: 72.308Å
α: 90° β: 104.64° γ: 90°
R-values:
R R work R free
0.119 0.118 0.132
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

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)
2 other articles

1 mention without citation

The Influence of Varying Fluorination Patterns on the Thermodynamics and Kinetics of Benzenesulfonamide Binding to Human Carbonic Anhydrase II.
Glöckner et al. (2020)