1zsc | pdb_00001zsc
CARBONIC ANHYDRASE II MUTANT E117Q, HOLO FORM
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Overview
Direct metal ligands to transition metals in metalloproteins exert a, profound effect on protein-metal affinity and function. Indirect ligands, i.e., second-shell residues that hydrogen bond to direct metal ligands, typically exert more subtle effects on the chemical properties of the, protein-metal complex. However, E117 of human carbonic anhydrase II, (CAII), which is part of the E117-119-Zn(2+) triad, is a notable, exception: E117-substituted CAIIs exhibit dramatically increased kinetics, of zinc complexation, and the E117Q variant exhibits enormously diminished, catalytic activity and sulfonamide affinity. The three-dimensional, structures of zinc-bound and zinc-free E117Q CAII reveal no discrete, structural changes in the active site that are responsible for enhanced, zinc ... [(full description)]
About this Structure
1ZSC is a [Single protein] structure of sequence from [Homo sapiens] with ZN as [ligand]. Active as [Carbonate dehydratase], with EC number [4.2.1.1]. Structure known Active Site: ZN. Full crystallographic information is available from [OCA].
Reference
Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II., Huang, CC, Lesburg CA, Kiefer LL, Fierke CA, Christianson DW, Biochemistry. 1996 Mar 19;35(11):3439-46. PMID:8639494
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