4gpi

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'''Unreleased structure'''
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{{STRUCTURE_4gpi| PDB=4gpi | SCENE= }}
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===Crystal structure of human B type phosphoglycerate mutase===
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{{ABSTRACT_PUBMED_23653202}}
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The entry 4gpi is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/PGAM1_HUMAN PGAM1_HUMAN]] Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.
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Authors: Zhou, L., He, C.
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==About this Structure==
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[[4gpi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GPI OCA].
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Description: Crystal structure of human B type phosphoglycerate mutase
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==Reference==
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<ref group="xtra">PMID:023653202</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: He, C.]]
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[[Category: Zhou, L.]]
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[[Category: Alpha/beta]]
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[[Category: Hydrolase]]
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[[Category: Isomerase]]

Revision as of 17:52, 19 June 2013

Template:STRUCTURE 4gpi

Contents

Crystal structure of human B type phosphoglycerate mutase

Template:ABSTRACT PUBMED 23653202

Function

[PGAM1_HUMAN] Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.

About this Structure

4gpi is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Hitosugi T, Zhou L, Fan J, Elf S, Zhang L, Xie J, Wang Y, Gu TL, Aleckovic M, Leroy G, Kang Y, Kang HB, Seo JH, Shan C, Jin P, Gong W, Lonial S, Arellano ML, Khoury HJ, Chen GZ, Shin DM, Khuri FR, Boggon TJ, Kang S, He C, Chen J. Tyr26 phosphorylation of PGAM1 provides a metabolic advantage to tumours by stabilizing the active conformation. Nat Commun. 2013;4:1790. doi: 10.1038/ncomms2759. PMID:23653202 doi:10.1038/ncomms2759

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