1vfd

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[[Image:1vfd.png|left|200px]]
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{{STRUCTURE_1vfd| PDB=1vfd | SCENE= }}
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===HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY GLU (R121E)===
===HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY GLU (R121E)===
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{{ABSTRACT_PUBMED_8931543}}
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==About this Structure==
==About this Structure==
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1VFD is a 1 chain structure of 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=1VFD OCA].
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[[1vfd]] is a 1 chain structure of [[Lactoferrin]] 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=1VFD OCA].
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==See Also==
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*[[Lactoferrin|Lactoferrin]]
==Reference==
==Reference==
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<ref group="xtra">PMID:8931543</ref><references group="xtra"/>
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<ref group="xtra">PMID:008931543</ref><ref group="xtra">PMID:015035615</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Baker, E N.]]
[[Category: Baker, E N.]]
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[[Category: Metal-binding]]
[[Category: Metal-binding]]
[[Category: Transferrin]]
[[Category: Transferrin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:35:18 2009''
 

Revision as of 06:33, 27 July 2012

Template:STRUCTURE 1vfd

Contents

HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY GLU (R121E)

Template:ABSTRACT PUBMED 8931543

About this Structure

1vfd is a 1 chain structure of Lactoferrin with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Faber HR, Baker CJ, Day CL, Tweedie JW, Baker EN. Mutation of arginine 121 in lactoferrin destabilizes iron binding by disruption of anion binding: crystal structures of R121S and R121E mutants. Biochemistry. 1996 Nov 19;35(46):14473-9. PMID:8931543 doi:10.1021/bi961729g
  • Flachner B, Kovari Z, Varga A, Gugolya Z, Vonderviszt F, Naray-Szabo G, Vas M. Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP. Biochemistry. 2004 Mar 30;43(12):3436-49. PMID:15035615 doi:10.1021/bi035022n

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