1bic

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spinqualitylabelsall models PDB ID 1bic Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.9Å
Ligands:	, and
Activity:	Carbonate dehydratase, with EC number 4.2.1.1
Coordinates:	save as pdb, mmCIF, xml

CRYSTALLOGRAPHIC ANALYSIS OF THR-200-> HIS HUMAN CARBONIC ANHYDRASE II AND ITS COMPLEX WITH THE SUBSTRATE, HCO3-

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

A complex of carbonic anhydrase (CA) with one of its substrates, bicarbonate, has been studied crystallographically. Human isoenzyme II was mutated at position 200 from threonine to histidine, which results in higher affinity for bicarbonate. The HCO3- ion binds in the active site to the zinc ion as a pseudo-bidentate ligand which gives the metal a coordination geometry between tetrahedral and trigonal bipyramide. The water/hydroxide normally bound with tetrahedral coordination to the zinc is probably replaced by the OH group of the bicarbonate ion. The importance of residues Thr-199 and Glu-106 in controlling the binding orientation of HCO3- is discussed as well as the catalytic mechanism. Both the complex as well as the uncomplexed mutant were studied at 1.9 A resolution.

Disease

Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]

About this Structure

1BIC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-., Xue Y, Vidgren J, Svensson LA, Liljas A, Jonsson BH, Lindskog S, Proteins. 1993 Jan;15(1):80-7. PMID:8451242

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