Structure of PDB 3swo Chain C

Receptor sequence
>3swoC (length=386) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
TYAPLELFDTDRLLDQDERDIAATVRQFVDTRLKPNVEGWFESATLPSEL
AKEFGNLGVLGMHLQGYGCAGTNAVSYGLACMELEAGDSGFRSFVSVQGS
LSMFSIYRYGSEEQKNEWLPRLAAGDAIGCFGLTEPDFGSNPAGMRTRAR
RDGSDWILNGTKMWITNGNLADVATVWAQTDDGIRGFLVPTDTPGFTANE
IHRKLSLRASVTSELVLDNVRLPASAQLPLAEGLSAPLSCLNEARFGIVF
GALGAARDSLETTIAYTQSREVFDKPLSNYQLTQEKLANMTVELGKGMLL
AIHLGRIKDAEGVRPEQISLGKLNNVREAIAIARECRTLLGGSGITLEYS
PLRHANNLESVLTYEGTSEMHLLSIGKALTGKAAFR
3D structure
PDB3swo Increasing the structural coverage of tuberculosis drug targets.
ChainC
Resolution1.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L143 T144 A254 E375 K387
Catalytic site (residue number reindexed from 1) L133 T134 A244 E365 K377
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 C R280 V282 F283 L287 Y290 T348 L349 G352 I355 R270 V272 F273 L277 Y280 T338 L339 G342 I345
BS02 FDA C F141 L143 T144 G149 S150 W174 I175 T176 T373 Y374 T377 E379 M380 F395 F131 L133 T134 G139 S140 W164 I165 T166 T363 Y364 T367 E369 M370 F385
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:3swo, PDBe:3swo, PDBj:3swo
PDBsum3swo
PubMed25613812
UniProtA0R6V6

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