Structure of PDB 4jq9 Chain F

Receptor sequence
>4jq9F (length=469) Species: 562 (Escherichia coli) [Search protein sequence]
STEIKTQVVVLGAGPAGYSAAFRCADLGLETVIVERYNTLGGVCLNVGCI
PSKALLHVAKVIEEAKALAEHGIVFGEPKTDIDKIRTWKEKVINQLTGGL
AGMAKGRKVKVVNGLGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPIQ
LPFIPHEDPRIWDSTDALELKEVPERLLVMGGGIIGLEMGTVYHALGSQI
DVVEMFDQVIPAADKDIVKVFTKRISKKFNLMLETKVTAVEAKEDGIYVT
MEGKKAPAEPQRYDAVLVAIGRVPNGKNLDAGKAGVEVDDRGFIRVDKQL
RTNVPHIFAIGDIVGQPMLAHKGVHEGHVAAEVIAGKKHYFDPKVIPSIA
YTEPEVAWVGLTEKEAKEKGISYETATFPWAASGRAIASDCADGMTKLIF
DKESHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHES
VGLAAEVFEGSITDLPNPK
3D structure
PDB4jq9 Dihydrolipoyl dehydrogenase of Escherichia coli pyruvate dehydrogenase complex
ChainF
Resolution2.17 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 F L12 G13 G15 P16 A17 E36 R37 V44 C45 G49 C50 K54 L116 G117 A145 G146 I186 D313 M319 L320 A321 H322 L11 G12 G14 P15 A16 E35 R36 V43 C44 G48 C49 K53 L115 G116 A144 G145 I185 D312 M318 L319 A320 H321
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004148 dihydrolipoyl dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
GO:0050660 flavin adenine dinucleotide binding

View graph for
Molecular Function
External links
PDB RCSB:4jq9, PDBe:4jq9, PDBj:4jq9
PDBsum4jq9
PubMed
UniProtC3TQA2

[Back to BioLiP]