1scz

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1scz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SCZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1scz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SCZ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e2o|1e2o]], [[1c4t|1c4t]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e2o|1e2o]], [[1c4t|1c4t]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SUCB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SUCB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </span></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/Dihydrolipoyllysine-residue_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1scz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1scz RCSB], [http://www.ebi.ac.uk/pdbsum/1scz PDBsum]</span></td></tr>
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<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=1scz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1scz RCSB], [http://www.ebi.ac.uk/pdbsum/1scz PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ODO2_ECOLI ODO2_ECOLI]] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
[[Category: Escherichia coli k-12]]
[[Category: Escherichia coli k-12]]
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[[Category: Arabashi, A.]]
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[[Category: Arabashi, A]]
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[[Category: Bunzel, B.]]
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[[Category: Bunzel, B]]
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[[Category: Carson, M.]]
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[[Category: Carson, M]]
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[[Category: DeLucas, L.]]
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[[Category: DeLucas, L]]
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[[Category: Gray, R.]]
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[[Category: Gray, R]]
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[[Category: Huang, W Y.]]
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[[Category: Huang, W Y]]
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[[Category: Johnson, D.]]
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[[Category: Johnson, D]]
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[[Category: Li, S.]]
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[[Category: Li, S]]
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[[Category: Lin, G.]]
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[[Category: Lin, G]]
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[[Category: Lu, S.]]
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[[Category: Lu, S]]
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[[Category: Luan, C H.]]
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[[Category: Luan, C H]]
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[[Category: Luo, D.]]
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[[Category: Luo, D]]
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[[Category: Luo, M.]]
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[[Category: Luo, M]]
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[[Category: Nagy, L.]]
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[[Category: Nagy, L]]
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[[Category: Pruett, P.]]
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[[Category: Pruett, P]]
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[[Category: Qiu, S.]]
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[[Category: Qiu, S]]
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[[Category: Schormann, N.]]
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[[Category: Schormann, N]]
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[[Category: Symersky, J.]]
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[[Category: Symersky, J]]
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[[Category: Tsao, J.]]
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[[Category: Tsao, J]]
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[[Category: Zhang, Z.]]
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[[Category: Zhang, Z]]
[[Category: Cat-like]]
[[Category: Cat-like]]
[[Category: Coa-dependent acyltransferase]]
[[Category: Coa-dependent acyltransferase]]
[[Category: Mixed beta-sheeet of 6 strand]]
[[Category: Mixed beta-sheeet of 6 strand]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 07:17, 25 December 2014

Improved structural model for the catalytic domain of E.coli dihydrolipoamide succinyltransferase

1scz, resolution 2.20Å

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