Structure of PDB 3owa Chain A

Receptor sequence
>3owaA (length=584) Species: 261594 (Bacillus anthracis str. 'Ames Ancestor') [Search protein sequence]
AVKGGSFLVDEITIDQVFTPEDFSSEHKMIAKTTEDFIVNEVLPELEYLE
QHEFDRSVRLLKEAGELGLLGADVPEEYGGIGLDKVSSALIAEKFSRAGG
FAITHGAHVGIGSLPIVLFGNEEQKKKYLPLLATGEKLAAYALTEPGSGS
DALGAKTTARLNAEGTHYVLNGEKQWITNSAFADVFIVYAKIDGEHFSAF
IVEKDYAGVSTSPEEKKMGIKCSSTRTLILEDALVPKENLLGEIGKGHII
AFNILNIGRYKLGVGTVGSAKRAVEISAQYANQRQQFKQPIARFPLIQEK
LANMAAKTYAAESSVYRTVGLFESRMSTLSEEEVKDGKAVAASIAEYAIE
CSLNKVFGSEVLDYTVDEGVQIHGGYGFMAEYEIERMYRDSRINRIFEGT
NEINRLIVPGTFLRKAMKGELPLLQKAQKLQEELMMMEVGDEPLALQKYL
VNNAKKIGLMVAGLAAQKYGKALDKEQEILVNIADIVSNLYAMESAVLRT
EKAIKTTGLEKNKQKVLYTEVFCQEAFNEIEAHAKETLIAVENGDMLRMM
LSSLRKLTRHTPLNVIPKKREIAAKILEDERYTV
3D structure
PDB3owa Crystal Structure of Acyl-CoA Dehydrogenase complexed with FAD from Bacillus anthracis
ChainA
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L150 T151 G265 E405 G417
Catalytic site (residue number reindexed from 1) L143 T144 G258 E398 G410
Enzyme Commision number 1.3.99.-
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 A Y148 L150 T151 G156 S157 W183 I184 T185 F404 T407 E409 I410 Q487 Y141 L143 T144 G149 S150 W176 I177 T178 F397 T400 E402 I403 Q477
BS02 FAD A R291 Q293 F294 F301 Q378 I379 G382 R284 Q286 F287 F294 Q371 I372 G375
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003995 acyl-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

View graph for
Molecular Function
External links
PDB RCSB:3owa, PDBe:3owa, PDBj:3owa
PDBsum3owa
PubMed
UniProtA0A6H3ADM7

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