Structure of PDB 5lnx Chain D

Receptor sequence
>5lnxD (length=374) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
MHVQEQVMMRKMVRDFARKEIAPAAEIMEKTDEFPFQLIKKMGKHGLMGI
PVPEQYGGAGADVVSYILAIHEISRISAAVGVILSVHTSVGTNPILYFGN
EEQKMKYIPNLASGDHLGAFALTEPHSGSDAGSLRTTAIKKNGKYLLNGS
KIFITNGGAADIYITFALTAPDQGRHGISAFIVEKNTPGFTVGKKERKLG
LYGSNTTELIFDNAEVPEANLLGKEGDGFHIAMANLNVGRIGIAAQALGI
AEAALEHAVDYAKQRVQFGRPIAANQGISFKLADMATRAEAARHLVYHAA
DLHNRLNCGKEASMAKQFASDAAVKALDAVQIYGGYGYMKDYPVERLLRD
AKVTQIYEGTNEIQRLIISKYLLG
3D structure
PDB5lnx Crystal structure of acyl-CoA dehydrogenase (MmgC) from bacillus subtilis.
ChainD
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L123 T124 G240 E360 K372
Catalytic site (residue number reindexed from 1) L122 T123 G239 E358 K370
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 D R266 Q268 F269 I273 N276 I279 Q333 I334 G337 R265 Q267 F268 I272 N275 I278 Q331 I332 G335
BS02 FAD D L123 T124 G129 S130 F154 T156 Y359 T362 E364 L122 T123 G128 S129 F153 T155 Y357 T360 E362
Gene Ontology
Molecular Function
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
Biological Process
GO:0030435 sporulation resulting in formation of a cellular spore
GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:5lnx, PDBe:5lnx, PDBj:5lnx
PDBsum5lnx
PubMed
UniProtP45857|ACDB_BACSU Acyl-CoA dehydrogenase (Gene Name=mmgC)

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