› 5lle

X-ray diffraction
1.9Å resolution

Crystal structure of human carbonic anhydrase isozyme II with 4-(1-Adamantylamino)-2,3,5,6-tetrafluorobenzenesulfonamide

Released:
DOI: 10.2210/pdb5lle/pdb
PDB entry 5lle coloured by chain, front view.
PDB entry 5lle coloured by chain, side view.
PDB entry 5lle coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding.
Smirnov A, Zubrienė A, Manakova E, Gražulis S, Matulis D
OpenAccess logo PeerJ 6 e4412 (2018)
PMID: 29503769

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: 260 amino acids
Theoretical weight: 29.29 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
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

5 bound ligands:
Ligand ZN 1 x ZN
Ligand V51 1 x V51
Ligand MES 1 x MES
Ligand DMS 1 x DMS
Ligand BCN 1 x BCN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 42.078Å b: 40.963Å c: 71.599Å
α: 90° β: 103.95° γ: 90°
R-values:
R R work R free
0.164 0.158 0.215
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

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

1 mention without citation

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