1i0e

From Proteopedia

(Difference between revisions)

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE==
-<StructureSection load='1i0e' size='340' side='right' caption='[[1i0e]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+<StructureSection load='1i0e' size='340' side='right'caption='[[1i0e]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1i0e]] is a 4 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=1I0E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I0E FirstGlance]. <br>
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 </div>
 <div class="pdbe-citations 1i0e" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Creatine kinase 3D structures|Creatine kinase 3D structures]]
 == References ==
 <references/>
@@ Line 34: / Line 37: @@
 [[Category: Creatine kinase]]
 [[Category: Homo sapiens]]
+[[Category: Large Structures]]
 [[Category: Lin, Z J]]
 [[Category: Shen, Y Q]]

Revision as of 07:08, 23 October 2019

CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE

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PDB ID 1i0e

Show:Asymmetric Unit Biological Assembly

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Structural highlights

1i0e is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Creatine kinase, with EC number 2.7.3.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KCRM_HUMAN] Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of human muscle creatine kinase has been determined by the molecular-replacement method and refined at 3.5A resolution. The structures of both the monomer and the dimer closely resemble those of the other known structures in the creatine kinase family. Two types of dimers, one with a non-crystallographic twofold symmetry axis and the other with a crystallographic twofold symmetry axis, were found to exist simultaneously in the crystal. These dimers form an infinite "double-helix"-like structure along an unusual long crystallographic 3(1) axis.

Structure of human muscle creatine kinase.,Shen YQ, Tang L, Zhou HM, Lin ZJ Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1196-200. PMID:11517911^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shen YQ, Tang L, Zhou HM, Lin ZJ. Structure of human muscle creatine kinase. Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1196-200. PMID:11517911

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

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1i0e

From Proteopedia

Revision as of 07:08, 23 October 2019

CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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