Structure of PDB 3d6b Chain C

Receptor sequence
>3d6bC (length=377) Species: 320372 (Burkholderia pseudomallei 1710b) [Search protein sequence]
ATFHWDDPLLLDQQLADDERMVRDAAHAYAQGKLAPRVTEAFRHETTDAA
IFREMGEIGLLGPTIPEQYGGPGLDYVSYGLIAREVERVDSGYRSMMSVQ
SSLVMVPIFEFGSDAQKEKYLPKLATGEWIGCFGLTEPNHGGSMVTRARK
VPGGYSLSGSKMWITNSPIADVFVVWAKLDEDGRDEIRGFILEKGCKGLS
APAIHGKVGLRASITGEIVLDEAFVPEENILPHVKGLRGPFTCLNSARYG
IAWGALGAAESCWHIARQYVLDRKQPLAANQLIQKKLADMQTEITLGLQG
VLRLGRMKDEGTAAVEITSIMKRNSCGKALDIARLARDMLGFGVARHLVN
LEVVNTYEGTHDIHALILGRAQTGIQA
3D structure
PDB3d6b Probing conformational states of glutaryl-CoA dehydrogenase by fragment screening.
ChainC
Resolution2.21 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L138 T139 A253 E374 R386
Catalytic site (residue number reindexed from 1) L135 T136 A247 E358 R370
Enzyme Commision number 1.3.8.6: glutaryl-CoA dehydrogenase (ETF).
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 54D C I257 Y373 E374 I251 Y357 E358
Gene Ontology
Molecular Function
GO:0000062 fatty-acyl-CoA binding
GO:0003995 acyl-CoA dehydrogenase activity
GO:0004361 glutaryl-CoA dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0046872 metal ion binding
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase
GO:0046949 fatty-acyl-CoA biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3d6b, PDBe:3d6b, PDBj:3d6b
PDBsum3d6b
PubMed21904051
UniProtQ3JP94

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