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1BWF

ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION

Summary for 1BWF
Entry DOI10.2210/pdb1bwf/pdb
DescriptorGLYCEROL KINASE, MAGNESIUM ION, PHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
Functional Keywordstransferase, kinase, domain motion, allosteric regulation hydrolase, lipid degradation, platelet factor
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight113838.14
Authors
Bystrom, C.E.,Pettigrew, D.W.,Branchaud, B.P.,Remington, S.J. (deposition date: 1998-09-23, release date: 1999-05-18, Last modification date: 2023-08-09)
Primary citationBystrom, C.E.,Pettigrew, D.W.,Branchaud, B.P.,O'Brien, P.,Remington, S.J.
Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion.
Biochemistry, 38:3508-3518, 1999
Cited by
PubMed: 10090737
DOI: 10.1021/bi982460z
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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