Dihydrolipoamide acetyltransferase
From Proteopedia
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==3D structures of dihydrolipoamide acetyltransferase== | ==3D structures of dihydrolipoamide acetyltransferase== | ||
| + | [[Dihydrolipoamide acetyltransferase 3D structures]] | ||
| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *DLAT lipoyl domain | ||
| - | |||
| - | **[[1lab]], [[1lac]] – GsDLAT lipoyl domain – ''Geobacillus stearothermophilus'' – NMR<BR /> | ||
| - | **[[1iyu]], [[1iyv]] - DLAT lipoyl domain – ''Azotobacter vinelandii'' – NMR<BR /> | ||
| - | **[[1fyc]] - DLAT lipoyl domain – human – NMR<BR /> | ||
| - | **[[1qjo]] - EcDLAT lipoyl domain – ''Escherichia coli'' – NMR<BR /> | ||
| - | |||
| - | *DLAT binding domain | ||
| - | |||
| - | **[[2pdd]], [[2pde]] – GsDLAT binding domain – NMR<BR /> | ||
| - | **[[1w4e]], [[1w4f]], [[1w4g]] - GsDLAT binding domain (mutant) – NMR<BR /> | ||
| - | **[[1w4h]] - EcDLAT binding domain – NMR<BR /> | ||
| - | **[[1w4i]] - PaDLAT binding domain – ''Pyrobaculum aerophilum'' – NMR<BR /> | ||
| - | **[[1w4j]], [[1w4k]] - PaDLAT binding domain (mutant) – NMR<BR /> | ||
| - | **[[1ebd]], [[2eq8]], [[2eq9]] - GsDLAT binding domain + E3<BR /> | ||
| - | **[[3rnm]] - hDLAT binding domain (mutant) + E3<BR /> | ||
| - | **[[1w85]], [[1w88]] - GsDLAT binding domain + E1<br /> | ||
| - | **[[1y8n]], [[1y8o]], [[1y8p]] - hDLAT binding domain + pyruvate dehydrogenase kinase | ||
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| - | *DLAT catalytic domain | ||
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| - | **[[1b5s]] - GsDLAT catalytic domain | ||
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| - | **[[2k7v]] – GsDLAT residues 206-293 – NMR<BR /> | ||
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| - | *Full DLAT | ||
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| - | **[[3duf]], [[3dv0]], [[3dva]] - GsDLAT + E1 | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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3D structures of dihydrolipoamide acetyltransferase
Dihydrolipoamide acetyltransferase 3D structures
References
- ↑ Lai WL, Chou LY, Ting CY, Kirby R, Tsai YC, Wang AH, Liaw SH. The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuation. J Biol Chem. 2004 Apr 2;279(14):13962-7. Epub 2004 Jan 21. PMID:14736882 doi:http://dx.doi.org/10.1074/jbc.M308849200
