3FE4

Crystal Structure of Human Carbonic Anhydrase vi

Summary for 3FE4

• Entry DOI: 10.2210/pdb3fe4/pdb
• Descriptor: Carbonic anhydrase 6, MAGNESIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: carbonic anhydrase, secretion, metal binding, structural genomics, structural genomics consortium, sgc, glycoprotein, lyase, metal-binding, secreted
• Biological source: Homo sapiens (Human)
• Cellular location: Secreted: P23280
• Total number of polymer chains: 2
• Total formula weight: 64133.81

Authors

Pilka, E.S.,Kochan, G.,Krysztofinska, E.,Muniz, J.,Yue, W.W.,Roos, A.K.,von Delft, F.,Arrowsmith, C.H.,Weigelt, J.,Edwards, A.,Bountra, C.,Oppermann, U.,Structural Genomics Consortium (SGC) (deposition date: 2008-11-27, release date: 2008-12-16, Last modification date: 2024-10-09)

Primary citation

Pilka, E.S.,Kochan, G.,Oppermann, U.,Yue, W.W.
Crystal structure of the secretory isozyme of mammalian carbonic anhydrases CA VI: implications for biological assembly and inhibitor development
Biochem.Biophys.Res.Commun., 419:485-489, 2012

PubMed Abstract: Zn(2+)-dependent carbonic anhydrases (CA) catalyse the reversible hydration of carbon dioxide to bicarbonate and participate in diverse physiological processes, hence having manifold therapeutic potentials. Among the 15 human CAs with wide-ranging sub-cellular localisation and kinetic properties, CA VI is the only secretory isoform. The 1.9Å crystal structure of the human CA VI catalytic domain reveals a prototypical mammalian CA fold, and a novel dimeric arrangement as compared to previously-reported CA structures. The active site cavity contains a cluster of non-conserved residues that may be involved in ligand binding and have significant implications for developing the next-generation of isoform-specific inhibitors.

PubMed: 22366092
DOI: 10.1016/j.bbrc.2012.02.038

Experimental method

X-RAY DIFFRACTION (1.9 Å)