1GLL
ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION
Summary for 1GLL
| Entry DOI | 10.2210/pdb1gll/pdb |
| Descriptor | GLYCEROL KINASE, MAGNESIUM ION, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | phosphotransferase, kinase, domain motion, allosteric regulation |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 113766.18 |
| Authors | Bystrom, C.E.,Pettigrew, D.W.,Branchaud, B.P.,Remington, S.J. (deposition date: 1998-09-24, release date: 1999-05-18, Last modification date: 2023-08-09) |
| Primary citation | Bystrom, 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: 10090737DOI: 10.1021/bi982460z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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