1abf: Difference between revisions

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[[Image:1abf.png|left|200px]]


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==SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES==
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<StructureSection load='1abf' size='340' side='right'caption='[[1abf]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1abf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ABF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ABF FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FCA:ALPHA-D-FUCOSE'>FCA</scene>, <scene name='pdbligand=FCB:BETA-D-FUCOSE'>FCB</scene></td></tr>
{{STRUCTURE_1abf|  PDB=1abf  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1abf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1abf OCA], [https://pdbe.org/1abf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1abf RCSB], [https://www.ebi.ac.uk/pdbsum/1abf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1abf ProSAT]</span></td></tr>
 
</table>
===SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES===
== Function ==
 
[https://www.uniprot.org/uniprot/ARAF_ECOLI ARAF_ECOLI] Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).
 
== Evolutionary Conservation ==
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{{ABSTRACT_PUBMED_2818726}}
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==About this Structure==
  </jmolCheckbox>
1ABF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ABF OCA].  
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1abf ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
Substrate specificity and affinity of a protein modulated by bound water molecules., Quiocho FA, Wilson DK, Vyas NK, Nature. 1989 Aug 3;340(6232):404-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2818726 2818726]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Quiocho, F A.]]
[[Category: Quiocho FA]]
[[Category: Wilson, D K.]]
[[Category: Wilson DK]]
[[Category: Binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:32:07 2008''

Latest revision as of 09:29, 7 February 2024

SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULESSUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES

Structural highlights

1abf is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARAF_ECOLI Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).

Evolutionary Conservation

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

1abf, resolution 1.90Å

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