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PDBe Entry: 2zeh view

Crystal structure of the human glutaminyl cyclase mutant E201Q at 1.8 angstrom resolution
Summary
Header TRANSFERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.8 Å, R-factor: 18.23%, Free R-factor: 20.7%, Spacegroup: H 3 2
Released 22/04/2008, deposition: 12/12/2007, last revision: 24/02/2009
Authors Huang, K.F.search; Wang, Y.R.search; Chang, E.C.search; Chou, T.L.search; Wang, A.H.search
Primary citation A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis.
BIOCHEM.J.search vol:411, pag:181-190 (2008) [PubMed ID 18072935 ]search
Keywords hydrogen bond networksearch, glutaminyl cyclasesearch, pyroglutamatesearch, site-directed mutagenesissearch, proton transfersearch, Acyltransferasesearch, Glycoproteinsearch, Metal-bindingsearch, Polymorphismsearch, Transferasesearch, Zincsearch
EC 2.3.2.5 ExPASy BRENDA search (A B)
Organism Homo sapiens(human) 9606search(A B)
UniProt Glutaminyl-peptide cyclotransferase precursor (EC 2.3.2.5) (Glutaminyl-tRNA cyclotransferase) (Glutaminyl cyclase) (QC) (Glutamyl cyclase) (EC) Q16769search (A B)
Solvent A, B
Related entries 2afm, 2zed, 2zee, 2zef, 2zeg, 2zel, 2zem, 2zen, 2zeo, 2zep
Polymers
Id Name Type UniProt Residues Observed
A, B Glutaminyl-peptide cyclotransferase Protein Q16769 (QPCT_HUMAN)search
329 98%
Heterogens
Id Name Ligands
A, B ZINC ION ZN search
A, B SULFATE ION SO4 search
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