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PDBe Entry: 1zs9 view

Crystal structure of human enolase-phosphatase E1
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.7 Å, R-factor: 20.8%, Free R-factor: 24.1%, Spacegroup: P 21 21 21
Released 21/06/2005, deposition: 23/05/2005, last revision: 24/02/2009
Authors Wang, H.search; Pang, H.search; Bartlam, M.search; Rao, Z.search
Primary citation Crystal Structure of Human E1 Enzyme and its Complex with a Substrate Analog Reveals the Mechanism of its Phosphatase/Enolase
J.MOL.BIOL.search vol:348, pag:917-926 (2005) [PubMed ID 15843022 ]search
Keywords STRUCTURE HUMAN ENOLASE-PHOSPHATASE E1search, HYDROLASEsearch
EC 3.1.3.77 ExPASy BRENDA search (A)
Organism Homo sapiens(human) 9606search(A)
UniProt Enolase-phosphatase E1 (EC 3.1.3.77) (2,3-diketo-5-methylthio-1-phosphopentane phosphatase) (MASA homolog) Q9UHY7search (A)
Solvent A
Related entries 1yns
Polymers
Id Name Type UniProt Residues Observed
A E-1 ENZYME Protein Q9UHY7 (ENOPH_HUMAN)search
261 96%
Heterogens
Id Name Ligands
A MAGNESIUM ION MG search
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