1hdi
From Proteopedia
(New page: 200px<br /> <applet load="1hdi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hdi, resolution 1.8Å" /> '''PIG MUSCLE 3-PHOSPHO...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1HDI is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] with MG, AMP and 3PG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HDI OCA]]. | + | 1HDI is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] with MG, AMP and 3PG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3]]. Structure known Active Sites: 3PG and AMP. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HDI OCA]]. |
==Reference== | ==Reference== | ||
A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure., Szilagyi AN, Ghosh M, Garman E, Vas M, J Mol Biol. 2001 Feb 23;306(3):499-511. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11178909 11178909] | A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure., Szilagyi AN, Ghosh M, Garman E, Vas M, J Mol Biol. 2001 Feb 23;306(3):499-511. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11178909 11178909] | ||
| + | [[Category: Phosphoglycerate kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: ternary complex]] | [[Category: ternary complex]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:02:52 2007'' |
Revision as of 11:58, 30 October 2007
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PIG MUSCLE 3-PHOSPHOGLYCERATE KINASE COMPLEXED WITH 3-PG AND MGADP.
Overview
3-phosphoglycerate kinase (PGK) is a typical kinase with two structural, domains. The domains each bind one of the two substrates, 3-phosphoglycerate (3-PG) and MgATP. For the phospho-transfer reaction to, take place the substrates must be brought closer by a hinge-bending domain, closure. Open and closed structures of the enzyme with different relative, domain positions have been determined from different species, but a, comprehensive description of this conformational transition is yet to be, attained. Crystals of pig muscle PGK in complex with MgADP and, 3-phosphoglycerate were grown under the conditions which have previously, resulted in crystals of the closed, catalytically competent conformation, of Trypanosoma brucei PGK. The X-ray structure of the pig muscle ternary, complex was ... [(full description)]
About this Structure
1HDI is a [Single protein] structure of sequence from [Sus scrofa] with MG, AMP and 3PG as [ligands]. Active as [Phosphoglycerate kinase], with EC number [2.7.2.3]. Structure known Active Sites: 3PG and AMP. Full crystallographic information is available from [OCA].
Reference
A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure., Szilagyi AN, Ghosh M, Garman E, Vas M, J Mol Biol. 2001 Feb 23;306(3):499-511. PMID:11178909
Page seeded by OCA on Tue Oct 30 14:02:52 2007
Categories: Phosphoglycerate kinase | Single protein | Sus scrofa | Garman, E. | Ghosh, M. | Szilagyi, A.N. | Vas, M. | 3PG | AMP | MG | Glycolysis | Kinase | Phosphoglycerate | Ternary complex
