› 3f7b

X-ray diffraction
2.05Å resolution

Crystal Structure of soluble domain of CA4 in complex with small molecule.

Released:
DOI: 10.2210/pdb3f7b/pdb
PDB entry 3f7b coloured by chain, front view.
PDB entry 3f7b coloured by chain, side view.
PDB entry 3f7b coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Thioether benzenesulfonamide inhibitors of carbonic anhydrases II and IV: structure-based drug design, synthesis, and biological evaluation.
Vernier W, Chong W, Rewolinski D, Greasley S, Pauly T, Shaw M, Dinh D, Ferre RA, Meador JW, Nukui S, Ornelas M, Paz RL, Reyner E
Bioorg Med Chem 18 3307-19 (2010)
PMID: 20363633

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
Molecule details ›
Chains: A, B
Length: 266 amino acids
Theoretical weight: 30.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

2 bound ligands:
Ligand ZN 2 x ZN
Ligand AG5 2 x AG5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 125.91Å b: 128.556Å c: 46.365Å
α: 90° β: 99.88° γ: 90°
R-values:
R R work R free
0.209 0.191 0.252
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)
14 other articles

2 mentions without citation

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