› 5lvs

X-ray diffraction
1.42Å resolution

Self-assembled protein-aromatic foldamer complexes with 2:3 and 2:2:1 stoichiometries

Released:
DOI: 10.2210/pdb5lvs/pdb
PDB entry 5lvs coloured by chain, front view.
PDB entry 5lvs coloured by chain, side view.
PDB entry 5lvs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Self-Assembled Protein-Aromatic Foldamer Complexes with 2:3 and 2:2:1 Stoichiometries.
Jewginski M, Granier T, Langlois d'Estaintot B, Fischer L, Mackereth CD, Huc I
J Am Chem Soc 139 2928-2931 (2017)
PMID: 28170240

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133686 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 259 amino acids
Theoretical weight: 29.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00918 (Residues: 2-260; Coverage: 100%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

8 bound ligands:
Ligand ZN 2 x ZN
Ligand 6H0 2 x 6H0
Ligand QUK 4 x QUK
Ligand QVS 2 x QVS
Ligand QVE 2 x QVE
Ligand GOL 12 x GOL
Ligand QUJ 4 x QUJ
Ligand FOR 1 x FOR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: C2
Unit cell:
a: 158.73Å b: 54.81Å c: 84.7Å
α: 90° β: 112.77° γ: 90°
R-values:
R R work R free
0.151 0.149 0.178
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

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

1 mention without citation

Variant ribosomal RNA alleles are conserved and exhibit tissue-specific expression.
Parks et al. (2018)