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2X15

The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP and 1,3- bisphosphoglycerate

Summary for 2X15
Entry DOI10.2210/pdb2x15/pdb
Related2WZB 2WZC 2WZD 2X13 2X14 2XE6 2XE7 2XE8 2Y3I
DescriptorPHOSPHOGLYCERATE KINASE 1, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
Functional Keywordstransition state analogue, hereditary hemolytic anemia, phosphoprotein, kinase, glycolysis, transferase, phosphoryl transfer, nucleotide-binding
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationCytoplasm: P00558
Total number of polymer chains1
Total formula weight45952.21
Authors
Bowler, M.W.,Cliff, M.J.,Marston, J.P.M.,Baxter, N.J.,Hounslow, A.M.H.,Varga, A.V.,Szabo, J.,Vas, M.,Blackburn, G.M.,Waltho, J.P. (deposition date: 2009-12-21, release date: 2011-02-09, Last modification date: 2023-12-20)
Primary citationBowler, M.W.,Cliff, M.J.,Marston, J.P.M.,Baxter, N.J.,Hounslow, A.M.H.,Varga, A.V.,Szabo, J.,Vas, M.,Blackburn, G.M.,Waltho, J.P.
The Structure of Human Phosphoglycerate Kinase in its Fully Active Conformation in Complex with Ground State Analoges
To be Published,
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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