› 5jeg

X-ray diffraction
1.19Å resolution

Human carbonic anhydrase II (V121I) complexed with benzo[d]thiazole-2-sulfonamide

Released:
DOI: 10.2210/pdb5jeg/pdb
PDB entry 5jeg coloured by chain, front view.
PDB entry 5jeg coloured by chain, side view.
PDB entry 5jeg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Water-Restructuring Mutations Can Reverse the Thermodynamic Signature of Ligand Binding to Human Carbonic Anhydrase.
Fox JM, Kang K, Sastry M, Sherman W, Sankaran B, Zwart PH, Whitesides GM
Angew Chem Int Ed Engl 56 3833-3837 (2017)
PMID: 28252841

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: B
Molecule details ›
Chain: B
Length: 259 amino acids
Theoretical weight: 29.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00918 (Residues: 3-260; Coverage: 99%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand EVF 2 x EVF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 42.43Å b: 41.48Å c: 72.64Å
α: 90° β: 104.64° γ: 90°
R-values:
R R work R free
0.133 0.132 0.156
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The Molecular Origin of Enthalpy/Entropy Compensation in Biomolecular Recognition.
Fox et al. (2018)
2 more