2ak3
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2ak3 |SIZE=350|CAPTION= <scene name='initialview01'>2ak3</scene>, resolution 1.85Å | |PDB= 2ak3 |SIZE=350|CAPTION= <scene name='initialview01'>2ak3</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Nucleoside-triphosphate--adenylate_kinase Nucleoside-triphosphate--adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.10 2.7.4.10] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-triphosphate--adenylate_kinase Nucleoside-triphosphate--adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.10 2.7.4.10] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ak3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ak3 OCA], [http://www.ebi.ac.uk/pdbsum/2ak3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ak3 RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Diederichs, K.]] | [[Category: Diederichs, K.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: AMP]] | ||
| - | [[Category: SO4]] | ||
[[Category: transferase (phosphotransferase)]] | [[Category: transferase (phosphotransferase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:53:46 2008'' |
Revision as of 22:53, 30 March 2008
| |||||||
| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Nucleoside-triphosphate--adenylate kinase, with EC number 2.7.4.10 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN MITOCHONDRIAL MATRIX ADENYLATE KINASE AND ITS SUBSTRATE AMP AT 1.85 ANGSTROMS RESOLUTION
Overview
The crystal structure of the complex between adenylate kinase from bovine mitochondrial matrix and its substrate AMP has been refined at 1.85 A resolution (1 A = 0.1 nm). Based on 42,519 independent reflections of better than 10 A resolution, a final R-factor of 18.9% was obtained with a model obeying standard geometry within 0.016 A in bond lengths and 3.2 degrees in bond angles. There are two enzyme: substrate complexes in the asymmetric unit, each consisting of 226 amino acid residues, one AMP and one sulfate ion. A superposition of the two full-length polypeptides revealed deviations that can be described as small relative movements of three domains. Best superpositions of individual domains yielded a residual overall root-mean-square deviation of 0.3 A for the backbone atoms and 0.5 A for the sidechains. The final model contains 381 solvent molecules in the asymmetric unit, 2 x 72 = 144 of which occupy corresponding positions in both complexes.
About this Structure
2AK3 is a Single protein structure of sequence from Bos taurus. This structure supersedes the now removed PDB entry 1AK3. Full crystallographic information is available from OCA.
Reference
The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 A resolution., Diederichs K, Schulz GE, J Mol Biol. 1991 Feb 5;217(3):541-9. PMID:1994037
Page seeded by OCA on Mon Mar 31 01:53:46 2008
