Structure of PDB 5u8w Chain B

Receptor sequence
>5u8wB (length=473) Species: 208963 (Pseudomonas aeruginosa UCBPP-PA14) [Search protein sequence]
SQKFDVVVIGAGPGGYVAAIRAAQLGLKTACIEKYIGKEGKVALGGTCLN
VGCIPSKALLDSSYKYHEAKEAFKVHGIEAKGVTIDVPAMVARKANIVKN
LTGGIATLFKANGVTSFEGHGKLLANKQVEVTGLDGKTQVLEAENVIIAS
GSRPVEIPPAPLTDDIIVDSTGALEFQAVPKKLGVIGAGVIGLELGSVWA
RLGAEVTVLEALDKFLPAADEQIAKEALKVLTKQGLNIRLGARVTASEVK
KKQVTVTFTDANGEQKETFDKLIVAVGRRPVTTDLLAADSGVTLDERGFI
YVDDHCKTSVPGVFAIGDVVRGAMLAHKASEEGVMVAERIAGHKAQMNYD
LIPSVIYTHPEIAWVGKTEQTLKAEGVEVNVGTFPFAASGRAMAANDTTG
LVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSH
PTLSEALHEAALAVNGHAIHIAN
3D structure
PDB5u8w The Pyruvate and alpha-Ketoglutarate Dehydrogenase Complexes of Pseudomonas aeruginosa Catalyze Pyocyanin and Phenazine-1-carboxylic Acid Reduction via the Subunit Dihydrolipoamide Dehydrogenase.
ChainB
Resolution1.79 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P14 L45 C49 C54 S57 G83 V84 V191 E195 S331 F449 H451 E456 N474
Catalytic site (residue number reindexed from 1) P13 L44 C48 C53 S56 G82 V83 V190 E194 S330 F448 H450 E455 N473
Enzyme Commision number 1.8.1.4: dihydrolipoyl dehydrogenase.
Interaction with ligand
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
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:5u8w, PDBe:5u8w, PDBj:5u8w
PDBsum5u8w
PubMed28174304
UniProtA0A0H2Z9F5

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