1ca2
From Proteopedia
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REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION
Contents |
Overview
The structure of human erythrocytic carbonic anhydrase II has been refined, by constrained and restrained structure-factor least-squares refinement at, 2.0 A resolution. The conventional crystallographic R value is 17.3%. Of, 167 solvent molecules associated with the protein, four are buried and, stabilize secondary structure elements. The zinc ion is ligated to three, histidyl residues and one water molecule in a nearly tetrahedral geometry., In addition to the zinc-bound water, seven more water molecules are, identified in the active site. Assuming that Glu-106 is deprotonated at pH, 8.5, some of the hydrogen bond donor-acceptor relations in the active site, can be assigned and are described here in detail. The O gamma 1 atom of, Thr-199 donates its proton to the O epsilon 1 atom of Glu-106 and can, function as a hydrogen bond acceptor only in additional hydrogen bonds.
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this Structure
1CA2 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. This structure superseeds the now removed PDB entry 1CAC. The following page contains interesting information on the relation of 1CA2 with [Carbonic Anhydrase]. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
Refined structure of human carbonic anhydrase II at 2.0 A resolution., Eriksson AE, Jones TA, Liljas A, Proteins. 1988;4(4):274-82. PMID:3151019
Page seeded by OCA on Mon Nov 12 16:18:52 2007
