› 4q49

Neutron Diffraction
1.8Å resolution

Room temperature neutron crystal structure of apo human carbonic anhydrase at pH 7.5

Released:
DOI: 10.2210/pdb4q49/pdb
PDB entry 4q49 coloured by chain, front view.
PDB entry 4q49 coloured by chain, side view.
PDB entry 4q49 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: 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 ZN 1 x ZN
Ligand DOD 188 x DOD
No modified residues

Experiments and Validation Details

Spacegroup: P21
Unit cell:
a: 42.78Å b: 41.71Å c: 72.82Å α: 90° β: 104.49° γ: 90°
R-values:
R R work R free 0.19 0.187 0.215
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

5 mentions without citation

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