1l8a

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spinqualitylabelsall models PDB ID 1l8a Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1l8a, resolution 1.85Å ()
Ligands:	,
Activity:	Pyruvate dehydrogenase (acetyl-transferring), with EC number 1.2.4.1
Structural annotation: Resources: CATH : 1L8Aa03, 1L8Ab03 InterPro : Ipr009014, Ipr004660, Ipr005474 Pfam : PF00456 SCOP : d1l8aa3, d1l8aa2, d1l8aa1, d1l8ab3, d1l8ab2, d1l8ab1 UniProt : P0AFG8
Functional annotation: Cellular component: membrane fraction Biological process: glycolysis Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity metal ion binding oxidoreductase activity magnesium ion binding protein binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

Contents 1 E. COLI PYRUVATE DEHYDROGENASE 2 About this Structure 3 See Also 4 Reference

E. COLI PYRUVATE DEHYDROGENASE

Template:ABSTRACT PUBMED 11955070

About this Structure

1l8a is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

• Pyruvate dehydrogenase

Reference

• Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Biochemistry. 2002 Apr 23;41(16):5213-21. PMID:11955070
• Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS. Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21. PMID:12651851 doi:http://dx.doi.org/10.1074/jbc.M300339200