1e4y: Difference between revisions
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|SITE= <scene name='pdbsite=AC1:Ap5+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Ap5+Binding+Site+For+Chain+B'>AC2</scene> | |SITE= <scene name='pdbsite=AC1:Ap5+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Ap5+Binding+Site+For+Chain+B'>AC2</scene> | ||
|LIGAND= <scene name='pdbligand=AP5:BIS(ADENOSINE)-5'-PENTAPHOSPHATE'>AP5</scene> | |LIGAND= <scene name='pdbligand=AP5:BIS(ADENOSINE)-5'-PENTAPHOSPHATE'>AP5</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4y OCA], [http://www.ebi.ac.uk/pdbsum/1e4y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e4y RCSB]</span> | |||
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[[Category: Mueller, C W.]] | [[Category: Mueller, C W.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
[[Category: transferase(phosphotransferase)]] | [[Category: transferase(phosphotransferase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:55:14 2008'' | ||
Revision as of 19:55, 30 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | Adenylate kinase, with EC number 2.7.4.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MUTANT P9L OF ADENYLATE KINASE FROM E. COLI, MODIFIED IN THE GLY-LOOP
OverviewOverview
Two mutants of adenylate kinase from Escherichia coli have been crystallized and analyzed by X-ray diffraction at resolutions of 3.4 and 2.4 A, respectively. These mutants are Pro-9-->Leu and Gly-10-->Val. They were selected for their positions in the highly conserved Gly-loop forming a giant anion hole for the beta-phosphate of ATP (GTP) in adenylate kinases, H-ras-p21, and other nucleotide-binding proteins. Mutants at these positions of H-ras-p21 cause cancer. In adenylate kinase these mutations cause smallish changes at the active site. Relating the structural changes to the known changes in catalysis indicates that these mutants hinder the induced-fit movements. As a side result we find that mutant Pro-9-->Leu and wild-type form one very similar crystal packing contact that is crystallographic in one case and noncrystallographic in the other, while all other packing contacts and the space groups are quite at variance.
About this StructureAbout this Structure
1E4Y is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop., Muller CW, Schulz GE, Proteins. 1993 Jan;15(1):42-9. PMID:8451239
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