› 6t81

X-ray diffraction
0.98Å resolution

Human Carbonic anhydrase II bound by 2-Naphthalenesulfonamide.

Released:
DOI: 10.2210/pdb6t81/pdb
PDB entry 6t81 coloured by chain, front view.
PDB entry 6t81 coloured by chain, side view.
PDB entry 6t81 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Isoform-Selective Enzyme Inhibitors by Exploring Pocket Size According to the Lock-and-Key Principle.
Dudutienė V, Zubrienė A, Kairys V, Smirnov A, Smirnovienė J, Leitans J, Kazaks A, Tars K, Manakova L, Gražulis S, Matulis D
Biophys J 119 1513-1524 (2020)
PMID: 32971003

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

Ligands and Environments

5 bound ligands:
Ligand ZN 1 x ZN
Ligand MUE 1 x MUE
Ligand BCN 1 x BCN
Ligand AZI 1 x AZI
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)
Spacegroup: P21
Unit cell:
a: 42.032Å b: 41.009Å c: 71.684Å
α: 90° β: 104.13° γ: 90°
R-values:
R R work R free
0.148 0.146 0.172
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Methyl 2-Halo-4-Substituted-5-Sulfamoyl-Benzoates as High Affinity and Selective Inhibitors of Carbonic Anhydrase IX.
Zakšauskas et al. (2021)
2 more

1 mention without citation

Isoform-Selective Enzyme Inhibitors by Exploring Pocket Size According to the Lock-and-Key Principle.
Dudutienė et al. (2020)