› 4y0j

Neutron Diffraction
2Å resolution

H/D exchanged human carbonic anhydrase II pH 6 room temperature neutron crystal structure.

Released:
DOI: 10.2210/pdb4y0j/pdb
PDB entry 4y0j coloured by chain, front view.
PDB entry 4y0j coloured by chain, side view.
PDB entry 4y0j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Joint neutron crystallographic and NMR solution studies of Tyr residue ionization and hydrogen bonding: Implications for enzyme-mediated proton transfer.
Michalczyk R, Unkefer CJ, Bacik JP, Schrader TE, Ostermann A, Kovalevsky AY, McKenna R, Fisher SZ
Proc Natl Acad Sci U S A 112 5673-8 (2015)
PMID: 25902526

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: 29.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

2 bound ligands:
Ligand ZN 1 x ZN
Ligand DOD 139 x DOD
No modified residues

Experiments and Validation Details

Spacegroup: P21
Unit cell:
a: 42.75Å b: 41.68Å c: 72.95Å α: 90° β: 104.67° γ: 90°
R-values:
R R work R free 0.263 0.263 0.291
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Neutron protein crystallography: A complementary tool for locating hydrogens in proteins.
O'Dell et al. (2016)
2 more

8 mentions without citation

Carbonic Anhydrases: Role in pH Control and Cancer.
Mboge et al. (2018)
7 more