Structure of PDB 3gqt Chain B

Receptor sequence

>3gqtB (length=372) Species: 320372 (Burkholderia pseudomallei 1710b)

ATFHWDDPLLLDQQLADDERMVRDAAHAYAQGKLAPRVTEAFRHETTDAA
IFREMGEIGLLGPTIPEQYGGPGLDYVSYGLIAREVERVDSGYRSMMSVQ
SSLVMVPIFEFGSDAQKEKYLPKLATGEWIGCFGLTEPMVTRARKVPGGY
SLSGSKMWITNSPIADVFVVWAKLDDEIRGFILEKGCKGLSAPAIHGKVG
LRASITGEIVLDEAFVPEENILPHVKGLRGPFTCLNSARYGIAWGALGAA
ESCWHIARQYVLDRKQFGRPLAANQLIQKKLADMQTEITLGLQGVLRLGR
MKDEGTAAVEITSIMKRNSCGKALDIARLARDMLGFGVARHLVNLEVVNT
YEGTHDIHALILGRAQTGIQAF

3D structure

• PDB: 3gqt Probing conformational states of glutaryl-CoA dehydrogenase by fragment screening.
• Chain: B
• Resolution: 1.99 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): L138 T139 A253 E374 R386
• Catalytic site (residue number reindexed from 1): L135 T136 A238 E352 R364
• 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	UFO	B	T139 L250 Y373 E374	T136 L235 Y351 E352
BS02	UFO	B	W169 T221 Y373	W158 T206 Y351

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

External links

• PDB: RCSB:3gqt, PDBe:3gqt, PDBj:3gqt
• PDBsum: 3gqt
• PubMed: 21904051
• UniProt: Q3JP94