› 7onv

X-ray diffraction
1.04Å resolution

Carbonic anhydrase II mutant (I91C) dually binding an IrCp* complex to generate an artificial transfer hydrogenase (ATHase)

Released:
DOI: 10.2210/pdb7onv/pdb
Model geometry
Fit model/data
PDB entry 7onv coloured by chain, front view.
PDB entry 7onv coloured by chain, side view.
PDB entry 7onv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A Dual Anchoring Strategy for the Directed Evolution of Improved Artificial Transfer Hydrogenases Based on Carbonic Anhydrase.
Stein A, Chen D, Igareta NV, Cotelle Y, Rebelein JG, Ward TR
OpenAccess logo ACS Cent Sci 7 1874-1884 (2021)
PMID: 34849402

Function and Biology Details

Reactions catalysed: 
hydrogencarbonate + H(+) = CO2 + H2O.
urea = cyanamide + H2O.
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: 261 amino acids
Theoretical weight: 29.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00918 (Residues: 1-1, 3-260; Coverage: 100%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand VKZ 1 x VKZ
Ligand EDO 9 x EDO
1 modified residue:
Ligand VI3 1 x VI3

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 42.278Å b: 71.807Å c: 73.694Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.2
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.
Van Stappen et al. (2022)
4 other articles