› 5dso

X-ray diffraction
1.4Å resolution

Structure of CO2 bound apo-form of human carbonic anhydrase II with 0 sec (no) warming

Released:
DOI: 10.2210/pdb5dso/pdb
PDB entry 5dso coloured by chain, front view.
PDB entry 5dso coloured by chain, side view.
PDB entry 5dso coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Tracking solvent and protein movement during CO2 release in carbonic anhydrase II crystals.
Kim CU, Song H, Avvaru BS, Gruner SM, Park S, McKenna R
Proc Natl Acad Sci U S A 113 5257-62 (2016)
PMID: 27114542

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
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 GOL 1 x GOL
Ligand CO2 2 x CO2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P21
Unit cell:
a: 42.104Å b: 41.168Å c: 71.744Å
α: 90° β: 104.36° γ: 90°
R-values:
R R work R free
0.114 0.112 0.159
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Catalytically Active Peptide-Gold Nanoparticle Conjugates: Prospecting for Artificial Enzymes.
Mikolajczak et al. (2020)
1 more

2 mentions without citation

Tracking solvent and protein movement during CO2 release in carbonic anhydrase II crystals.
Kim et al. (2016)
1 more