Structure of PDB 6cmz Chain D

Receptor sequence
>6cmzD (length=459) Species: 216591 (Burkholderia cenocepacia J2315) [Search protein sequence]
KNEHTTLLVIGGGPGGYVAAIRAGQLGIPTVLVERDRLGGTCLNIGCIPS
KALIHVADAFEQACGHAGEGALGIRVRAPEIDIAKSVAWKDGIVDRLTRG
VGALLKKSGVRVLHGEARVIDGKTVEVVSAGHAVRIGCEHLLLATGSEPV
ELPSMPFGGHVVSSTDALSPATLPKRLVVVGAGYIGLELGIVYRKLGVDV
SVVEAAERVLPAYDAELVRPVADSLARLGVRLWLGHKVLGLDKHGAVRVQ
AADGAEQTLPADRVLVAVGRRPRVDGFGLETLMLDRNGRALRIDDTCRTS
MRNVWAIGDVAGEPMLAHRAMAQGEMVAELIAGRRRQFMPAAIPAVCFTD
PEIVTAGWSPDDAHAAGVDCLSASFPFAANGRAMTLQATDGFVRVVARRD
NHLIVGWQAVGRGVSELAAAFSQSLEMGARLEDIGGTIHAHPTLGEALQE
AALRALGHA
3D structure
PDB6cmz 2.3 Angstrom Resolution Crystal Structure of Dihydrolipoamide Dehydrogenase from Burkholderia cenocepacia in Complex with FAD and NAD.
ChainD
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C43 C48 S51 Y185 E189 H442 E447
Catalytic site (residue number reindexed from 1) C42 C47 S50 Y184 E188 H441 E446
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 D G14 P15 E35 R36 G41 T42 C43 G47 C48 K52 A118 T146 G147 Y185 I186 R271 F278 G309 D310 M316 L317 A318 H319 G13 P14 E34 R35 G40 T41 C42 G46 C47 K51 A117 T145 G146 Y184 I185 R270 F277 G308 D309 M315 L316 A317 H318
BS02 ADP D G182 E205 A206 V269 G181 E204 A205 V268
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:6cmz, PDBe:6cmz, PDBj:6cmz
PDBsum6cmz
PubMed
UniProtB4EEF2

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