Structure of PDB 4jdr Chain B

Receptor sequence
>4jdrB (length=471) Species: 562 (Escherichia coli) [Search protein sequence]
STEIKTQVVVLGAGPAGYSAAFRCADLGLETVIVERYNTLGGVCLNVGCI
PSKALLHVAKVIEEAKALAEHGIVFGEPKTDIDKIRTWKEKVINQLTGGL
AGMAKGRKVKVVNGLGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPIQ
LPFIPHEDPRIWDSTDALELKEVPERLLVMGGGIIGLEMGTVYHALGSQI
DVVEMFDQVIPAADKDIVKVFTKRISKKFNLMLETKVTAVEAKEDGIYVT
MEGKKAPAEPQRYDAVLVAIGRVPNGKNLDAGKAGVEVDDRGFIRVDKQL
RTNVPHIFAIGDIVGQPMLAHKGVHEGHVAAEVIAGKKHYFDPKVIPSIA
YTEPEVAWVGLTEKEAKEKGISYETATFPWAASGRAIASDCADGMTKLIF
DKESHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHES
VGLAAEVFEGSITDLPNPKAK
3D structure
PDB4jdr Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural Approaches.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P16 L41 C45 C50 S53 E78 P79 I185 E189 V325 H443 H445 E450 N468 P469
Catalytic site (residue number reindexed from 1) P15 L40 C44 C49 S52 E77 P78 I184 E188 V324 H442 H444 E449 N467 P468
Enzyme Commision number 1.8.1.4: dihydrolipoyl dehydrogenase.
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 FAD B G13 G15 P16 A17 E36 R37 Y38 V44 C45 G49 C50 K54 L116 G117 A145 G146 I186 G312 D313 M319 L320 A321 H322 G12 G14 P15 A16 E35 R36 Y37 V43 C44 G48 C49 K53 L115 G116 A144 G145 I185 G311 D312 M318 L319 A320 H321
Gene Ontology
Molecular Function
GO:0004148 dihydrolipoyl dehydrogenase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0015036 disulfide oxidoreductase activity
GO:0016491 oxidoreductase activity
GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
GO:0042802 identical protein binding
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0006090 pyruvate metabolic process
GO:0006099 tricarboxylic acid cycle
GO:0006103 2-oxoglutarate metabolic process
GO:0006730 one-carbon metabolic process
GO:0006979 response to oxidative stress
GO:0019464 glycine decarboxylation via glycine cleavage system
GO:0042867 pyruvate catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005960 glycine cleavage complex
GO:0016020 membrane
GO:0045252 oxoglutarate dehydrogenase complex
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:4jdr, PDBe:4jdr, PDBj:4jdr
PDBsum4jdr
PubMed23580650
UniProtP0A9P0|DLDH_ECOLI Dihydrolipoyl dehydrogenase (Gene Name=lpdA)

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