1AKE
STRUCTURE OF THE COMPLEX BETWEEN ADENYLATE KINASE FROM ESCHERICHIA COLI AND THE INHIBITOR AP5A REFINED AT 1.9 ANGSTROMS RESOLUTION: A MODEL FOR A CATALYTIC TRANSITION STATE
Summary for 1AKE
Entry DOI | 10.2210/pdb1ake/pdb |
NMR Information | BMRB: 5720,5746 |
Descriptor | ADENYLATE KINASE, BIS(ADENOSINE)-5'-PENTAPHOSPHATE (3 entities in total) |
Functional Keywords | transferase(phosphotransferase) |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P69441 |
Total number of polymer chains | 2 |
Total formula weight | 49072.79 |
Authors | Mueller, C.W.,Schulz, G.E. (deposition date: 1991-11-08, release date: 1994-01-31, Last modification date: 2024-06-05) |
Primary citation | Muller, C.W.,Schulz, G.E. Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state. J.Mol.Biol., 224:159-177, 1992 Cited by PubMed: 1548697DOI: 10.1016/0022-2836(92)90582-5 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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