Structure of PDB 3sf6 Chain A

Receptor sequence
>3sf6A (length=387) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
RRGADDLIGINAVLSAEEREIRDTVRSVVQRRIKPHIASWYEDGELPARE
LAVELGELGLLGMHLKGYGCAGMSAVAYGLACLELEAGDSGIRSLVSVQG
SLAMYAIHAFGSDEQKDQWLPDMASGHRIGCFGLTEPDHGSDPAGMRTRA
TRSGDDWILTGTKMWITNGSVADVAVVWARTDEGIRGFVVPTDTPGFTAN
TIKSKMSLRASVTSELVLDGVRLPDSARLPGATSLGAPLRCLNEARFGIV
FGALGAARDCLETALAYACSREQFDRPIGGFQLTQQKLADMTLEYGKGFL
LALHLGRQKDAGELAPEQVSLGKLNNVREAIEIARTARTVLGASGITGEY
PVMRHANNLESVLTYEGTSEMHTLIIGQALTGVGAFR
3D structure
PDB3sf6 Increasing the structural coverage of tuberculosis drug targets.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L146 T147 A257 E378 Q390
Catalytic site (residue number reindexed from 1) L134 T135 A245 E366 Q378
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 FDA A F144 L146 T147 G152 S153 W177 I178 T179 S373 T376 Y377 T380 E382 M383 F132 L134 T135 G140 S141 W165 I166 T167 S361 T364 Y365 T368 E370 M371
Gene Ontology
Molecular Function
GO:0000062 fatty-acyl-CoA binding
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3sf6, PDBe:3sf6, PDBj:3sf6
PDBsum3sf6
PubMed25613812
UniProtA0QV68

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