› 4lp6

X-ray diffraction
2.15Å resolution

Crystal Structure of Human Carbonic Anhydrase II in complex with a quinoline oligoamide foldamer

Released:
DOI: 10.2210/pdb4lp6/pdb
PDB entry 4lp6 coloured by chain, front view.
PDB entry 4lp6 coloured by chain, side view.
PDB entry 4lp6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a complex formed by a protein and a helical aromatic oligoamide foldamer at 2.1 Å resolution.
Buratto J, Colombo C, Stupfel M, Dawson SJ, Dolain C, Langlois d'Estaintot B, Fischer L, Granier T, Laguerre M, Gallois B, Huc I
Angew Chem Int Ed Engl 53 883-7 (2014)
PMID: 24288253

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-133681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 2 Chains: A, B
Molecule details ›
Chains: A, B
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

2 bound ligands:
Ligand Q4I 2 x Q4I
Ligand ZN 13 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 45.96Å b: 84.17Å c: 76.7Å
α: 90° β: 97.18° γ: 90°
R-values:
R R work R free
0.194 0.191 0.253
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Handedness preference and switching of peptide helices. Part I: Helices based on protein amino acids.
De Zotti et al. (2014)
2 more

1 mention without citation

Supramolecular Chemistry Targeting Proteins.
van Dun et al. (2017)