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1s4p

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Current revision (06:12, 23 August 2023) (edit) (undo)
 
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<StructureSection load='1s4p' size='340' side='right'caption='[[1s4p]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
<StructureSection load='1s4p' size='340' side='right'caption='[[1s4p]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1s4p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S4P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1s4p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S4P FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KRE2, MNT1, YDR483W, D8035.26 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/GDP-Man:Man(3)GlcNAc(2)-PP-dolichol_alpha-1,2-mannosyltransferase GDP-Man:Man(3)GlcNAc(2)-PP-dolichol alpha-1,2-mannosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.131 2.4.1.131] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4p OCA], [https://pdbe.org/1s4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s4p RCSB], [https://www.ebi.ac.uk/pdbsum/1s4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4p ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1s4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4p OCA], [http://pdbe.org/1s4p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s4p RCSB], [http://www.ebi.ac.uk/pdbsum/1s4p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4p ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KRE2_YEAST KRE2_YEAST]] Required for the attachment of the third mannose residue of O-linked saccharides.
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[https://www.uniprot.org/uniprot/KRE2_YEAST KRE2_YEAST] Required for the attachment of the third mannose residue of O-linked saccharides.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Herscovics, A]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Howell, P L]]
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[[Category: Herscovics A]]
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[[Category: Lobsanov, Y D]]
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[[Category: Howell PL]]
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[[Category: Romero, P A]]
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[[Category: Lobsanov YD]]
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[[Category: Sleno, B]]
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[[Category: Romero PA]]
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[[Category: Yip, P]]
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[[Category: Sleno B]]
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[[Category: Yu, B]]
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[[Category: Yip P]]
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[[Category: Alpha/beta fold]]
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[[Category: Yu B]]
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[[Category: Nucleotide-binding domain]]
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[[Category: Rossmann fold]]
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[[Category: Ternary complex with gdp-mn2+ and methyl-alpha-mannoside acceptor]]
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[[Category: Transferase]]
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Current revision

Crystal structure of yeast alpha1,2-mannosyltransferase Kre2p/Mnt1p: ternary complex with GDP/Mn and methyl-alpha-mannoside acceptor

PDB ID 1s4p

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