Structure of PDB 2qta Chain B

Receptor sequence
>2qtaB (length=801) Species: 562 (Escherichia coli) [Search protein sequence]
ISNYINTIPVEEQPEYPGNLELERRIRSAIRWNAIMTVLRASKKDLELGG
HMASFQSSATIYDVCFNHFFRARNEQDGGDLVYFQGHISPGVYARAFLEG
RLTQEQLDNFRQEVHGNGLSSYPHPKLMPEFWQFPTVSMGLGPIGAIYQA
KFLKYLEHRGLKDTSKQTVYAFLGDGEMDEPESKGAITIATREKLDNLVF
VINCNLQRLDGPVTGNGKIINELEGIFEGAGWNVIKVMWGSRWDELLRKD
TSGKLIQLMNETVDGDYQTFKSKDGAYVREHFFGKYPETAALVADWTDEQ
IWALNRGGHDPKKIYAAFKKAQETKGKATVILAHTIKGYGMGDAAMDGVR
HIRDRFNVPVSDADIEKLPYITFPEGSEEHTYLHAQRQKLHGYLPSRQPN
FTEKLELPSLQDFGALLEEQSKEISTTIAFVRALNVMLKNKSIKDRLVPI
IADEARTFGMEGLFRQIGIYSPEDEKGQILQEGINELGAGCSWLAAATSY
STNNLPMIPFYIYYSMFGFQRIGDLCWAAGDQQARGFLIGGTSGRTTLNG
EGLQHEDGHSHIQSLTIPNCISYDPAYAYEVAVIMHDGLERMYGEKQENV
YYYITTLNENYHMPAMPEGAEEGIRKGIYKLETIEGSKGKVQLLGSGSIL
RHVREAAEILAKDYGVGSDVYSVTSFTELARDGQDCERWNMLHPLETPRV
PYIAQVMNDAPAVASTDYMKLFAEQVRTYVPADDYRVLGTDGFGRSDSRE
NLRHHFEVDASYVVVAALGELAKRGEIDKKVVADAIAKFNIDADKVNPRL
A
3D structure
PDB2qta A Dynamic Loop at the Active Center of the Escherichia coli Pyruvate Dehydrogenase Complex E1 Component Modulates Substrate Utilization and Chemical Communication with the E2 Component
ChainB
Resolution1.85 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.2.4.1: pyruvate dehydrogenase (acetyl-transferring).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 TPP B E522 I569 E571 F602 E454 I484 E486 F517
BS02 MG B D230 N260 Q262 D175 N205 Q207
BS03 TPP B S109 Q140 H142 V192 M194 G229 D230 G231 E232 N260 Q262 R263 L264 K392 S54 Q85 H87 V137 M139 G174 D175 G176 E177 N205 Q207 R208 L209 K337
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004738 pyruvate dehydrogenase activity
GO:0004739 pyruvate dehydrogenase (acetyl-transferring) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0030976 thiamine pyrophosphate binding
GO:0036094 small molecule binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0060090 molecular adaptor activity
Biological Process
GO:0042867 pyruvate catabolic process
Cellular Component
GO:0005829 cytosol
GO:0016020 membrane
GO:0045254 pyruvate dehydrogenase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2qta, PDBe:2qta, PDBj:2qta
PDBsum2qta
PubMed17635929
UniProtP0AFG8|ODP1_ECOLI Pyruvate dehydrogenase E1 component (Gene Name=aceE)

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