› 4ygk

X-ray diffraction
1.5Å resolution

NaSCN--Interactions between Hofmeister Anions and the Binding Pocket of a Protein

Released:
DOI: 10.2210/pdb4ygk/pdb
PDB entry 4ygk coloured by chain, front view.
PDB entry 4ygk coloured by chain, side view.
PDB entry 4ygk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Interactions between Hofmeister anions and the binding pocket of a protein.
Fox JM, Kang K, Sherman W, Héroux A, Sastry GM, Baghbanzadeh M, Lockett MR, Whitesides GM
J Am Chem Soc 137 3859-66 (2015)
PMID: 25738615

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: 258 amino acids
Theoretical weight: 29 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

3 bound ligands:
Ligand ZN 1 x ZN
Ligand SCN 1 x SCN
Ligand OH 1 x OH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 42.391Å b: 41.346Å c: 72.912Å
α: 90° β: 104.7° γ: 90°
R-values:
R R work R free
0.175 0.173 0.213
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Reconsidering anion inhibitors in the general context of drug design studies of modulators of activity of the classical enzyme carbonic anhydrase.
Nocentini et al. (2021)
12 more

1 mention without citation

Interactions between Hofmeister anions and the binding pocket of a protein.
Fox et al. (2015)