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<StructureSection load='4atm' size='340' side='right'caption='[[4atm]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
<StructureSection load='4atm' size='340' side='right'caption='[[4atm]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4atm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4a3a 4a3a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ATM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ATM FirstGlance]. <br>
<table><tr><td colspan='2'>[[4atm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4a3a 4a3a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ATM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ATM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.783&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ky7|1ky7]], [[1utc|1utc]], [[4a3a|4a3a]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4atm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atm OCA], [http://pdbe.org/4atm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4atm RCSB], [http://www.ebi.ac.uk/pdbsum/4atm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4atm ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4atm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atm OCA], [https://pdbe.org/4atm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4atm RCSB], [https://www.ebi.ac.uk/pdbsum/4atm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4atm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/AMPH_HUMAN AMPH_HUMAN]] May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton.  
[https://www.uniprot.org/uniprot/AMPH_HUMAN AMPH_HUMAN] May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton.
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Allerston, C K]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Allerston CK]]
[[Category: Bountra, C]]
[[Category: Arrowsmith CH]]
[[Category: Delft, F von]]
[[Category: Bountra C]]
[[Category: Edwards, A]]
[[Category: Edwards A]]
[[Category: Gileadi, O]]
[[Category: Gileadi O]]
[[Category: Krojer, T]]
[[Category: Krojer T]]
[[Category: Weigelt, J]]
[[Category: Weigelt J]]
[[Category: Invagination]]
[[Category: Von Delft F]]
[[Category: Knobs-in-hole]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural protein]]

Latest revision as of 14:35, 20 December 2023

Crystal structure of the BAR domain of human Amphiphysin, isoform 1 at 1.8 Angstrom resolution featuring increased order at the N- terminus.Crystal structure of the BAR domain of human Amphiphysin, isoform 1 at 1.8 Angstrom resolution featuring increased order at the N- terminus.

Structural highlights

4atm is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 4a3a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.783Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMPH_HUMAN May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton.

4atm, resolution 1.78Å

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OCA