Structure of PDB 2eba Chain H

Receptor sequence

>2ebaH (length=380) Species: 300852 (Thermus thermophilus HB8)

MLDFYALEDLLTPEEKEVQKAARRFLEKEALPHIRDWWEEGVFPTHLIPR
FAELGFLGPTLPPEYGGAGVSSAAYGLICYELERVDSGLRSFVSVQSSLV
MYPIYAYGSEEQKREFLPKLARGEMVGCFGLTEPDGGSDPYGNMKTRARR
DTWVLNGTKMWITNGNLAHLAVIWAKDEVLGFLVPTDTPGFQAREVKRKM
SLRASVTSELVLEEVRVPESLRLPKALGLKAPLSCLTQARFGIAWGAMGA
LEAVYEEAVAFAKSRSTFGEPLAKKQLVQAKLAEMLAWHTEGLLLAWRLA
RLKDEGKLTPAQVSLAKRQNVWKALQAARMARDILGGSGITLEYHAIRHM
LNLETVYTYEGTHDVHTLVLGREITGLNAF

3D structure

• PDB: 2eba Crystal structure of the putative glutaryl-CoA dehydrogenase from thermus thermophilus
• Chain: H
• Resolution: 2.21 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): L131 T132 A244 E365 R377
• Catalytic site (residue number reindexed from 1): L131 T132 A239 E360 R372
• 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	FAD	H	L131 T132 G136 G137 S138 W163 T165 T360 T363 Y364 T367	L131 T132 G136 G137 S138 W161 T163 T355 T358 Y359 T362
BS02	FAD	H	R270 T272 L277 K280 D338 I339 G342	R265 T267 L272 K275 D333 I334 G337

Gene Ontology

Molecular Function

• GO:0000062 fatty-acyl-CoA binding
• GO:0000166 nucleotide 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: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:2eba, PDBe:2eba, PDBj:2eba
• PDBsum: 2eba
• UniProt: Q5SK63