› 5jna

X-ray diffraction
2Å resolution

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-149789 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 266 amino acids
Theoretical weight: 30.36 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P22748 (Residues: 19-284; Coverage: 91%)
Gene name: CA4
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

5 bound ligands:
Ligand ZN 4 x ZN
Ligand TOR 4 x TOR
Ligand SO4 8 x SO4
Ligand GOL 3 x GOL
Ligand ACT 3 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 64.908Å b: 123.798Å c: 151.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.172 0.218
Expression system: Cricetulus griseus

Quick links

Citations

1 review citation

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

1 mention without citation

Intrinsic thermodynamics of high affinity inhibitor binding to recombinant human carbonic anhydrase IV.
Mickevičiūtė et al. (2018)