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2X14

The catalytically active fully closed conformation of human phosphoglycerate kinase K219A mutant in complex with AMP-PCP and 3PG

Summary for 2X14
Entry DOI10.2210/pdb2x14/pdb
Related2WZB 2WZC 2WZD 2X13 2X15 2XE6 2XE7 2XE8 2Y3I
DescriptorPHOSPHOGLYCERATE KINASE 1, MAGNESIUM ION, 3-PHOSPHOGLYCERIC ACID, ... (5 entities in total)
Functional Keywordstransition state analogue, hereditary hemolytic anemia, atp-binding, kinase, glycolysis, transferase, disease mutation
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationCytoplasm: P00558
Total number of polymer chains1
Total formula weight45198.89
Authors
Bowler, M.W.,Cliff, M.J.,Marston, J.P.M.,Baxter, N.J.,Hownslow, A.M.H.,Varga, A.V.,Szabo, J.,Vas, M.,Blackburn, G.M.,Waltho, J.P. (deposition date: 2009-12-21, release date: 2010-12-29, Last modification date: 2023-12-20)
Primary citationBowler, M.W.,Cliff, M.J.,Marston, J.P.M.,Baxter, N.J.,Hownslow, 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 Analogues
To be Published,
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

217705

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