› 1z97

X-ray diffraction
2.1Å resolution

Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer.

Released:
DOI: 10.2210/pdb1z97/pdb
PDB entry 1z97 coloured by chain, front view.
PDB entry 1z97 coloured by chain, side view.
PDB entry 1z97 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer.
Duda DM, Tu C, Fisher SZ, An H, Yoshioka C, Govindasamy L, Laipis PJ, Agbandje-McKenna M, Silverman DN, McKenna R
Biochemistry 44 10046-53 (2005)
PMID: 16042381

Function and Biology Details

Reaction catalysed: 
H(2)CO(3) = CO(2) + 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-139595 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 3 Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 30.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07451 (Residues: 1-260; Coverage: 100%)
Gene name: CA3
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 44.105Å b: 70.775Å c: 44.487Å
α: 90° β: 115.07° γ: 90°
R-values:
R R work R free
0.186 0.186 0.237
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
Krishnamurthy et al. (2008)
11 more