This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3c7q
From Proteopedia
| Line 1: | Line 1: | ||
| + | |||
==Structure of VEGFR2 kinase domain in complex with BIBF1120== | ==Structure of VEGFR2 kinase domain in complex with BIBF1120== | ||
<StructureSection load='3c7q' size='340' side='right' caption='[[3c7q]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3c7q' size='340' side='right' caption='[[3c7q]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3c7q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3c7q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C7Q FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XIN:METHYL+(3Z)-3-{[(4-{METHYL[(4-METHYLPIPERAZIN-1-YL)ACETYL]AMINO}PHENYL)AMINO](PHENYL)METHYLIDENE}-2-OXO-2,3-DIHYDRO-1H-INDOLE-6-CARBOXYLATE'>XIN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XIN:METHYL+(3Z)-3-{[(4-{METHYL[(4-METHYLPIPERAZIN-1-YL)ACETYL]AMINO}PHENYL)AMINO](PHENYL)METHYLIDENE}-2-OXO-2,3-DIHYDRO-1H-INDOLE-6-CARBOXYLATE'>XIN</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KDR, FLK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KDR, FLK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></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=3c7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c7q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c7q RCSB], [http://www.ebi.ac.uk/pdbsum/3c7q PDBsum]</span></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=3c7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c7q OCA], [http://pdbe.org/3c7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c7q RCSB], [http://www.ebi.ac.uk/pdbsum/3c7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c7q ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
| Line 21: | Line 22: | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </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/ | + | </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=3c7q ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 31: | Line 32: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3c7q" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| Line 38: | Line 40: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: Receptor protein-tyrosine kinase]] | [[Category: Receptor protein-tyrosine kinase]] | ||
[[Category: Bader, G]] | [[Category: Bader, G]] | ||
Revision as of 20:04, 11 August 2016
Structure of VEGFR2 kinase domain in complex with BIBF1120
| |||||||||||
Categories: Human | Receptor protein-tyrosine kinase | Bader, G | Garin-Chesa, P | Heckel, A | Hilberg, F | Kautschitsch, S | Krssak, M | Quant, J | Rettig, W J | Roth, G J | Sommergruber, W | Tontsch-Grunt, U | Zoephel, A | Alpha beta | Angiogenesis | Atp-binding | Developmental protein | Differentiation | Glycoprotein | Host-virus interaction | Immunoglobulin domain | Kinase | Membrane | Nucleotide-binding | Phosphoprotein | Receptor | Transferase | Transmembrane | Tyrosine-protein kinase


