Structure of PDB 5lnx Chain A

Receptor sequence
>5lnxA (length=367) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
EQVMMRKMVRDFARKEIAPAAEIMEKTDEFPFQLIKKMGKHGLMGIPVPE
QYGGAGADVVSYILAIHEISRISAAVGVILSVHTSVGTNPILYFGNEEQK
MKYIPNLASGDHLGAFALTEPHSGSDAGSLRTTAIKKGKYLLNGSKIFIT
NGGAADIYITFALTAPDQGRHGISAFIVEKNTPGFTVGKKERKLGLYGSN
TTELIFDNAEVPEANLLGKEGDGFHIAMANLNVGRIGIAAQALGIAEAAL
EHAVDYAKQRVQFGRPIAANQGISFKLADMATRAEAARHLVYHAADLHNG
LNCGKEASMAKQFASDAAVKALVQIYGGYGYMKDYPVERLLRDAKVTQIY
EGTNEIQRLIISKYLLG
3D structure
PDB5lnx Crystal structure of acyl-CoA dehydrogenase (MmgC) from bacillus subtilis.
ChainA
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) L118 T119 G234 E351 K363
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 F121 L123 T124 G129 S130 F154 T156 Y359 T362 E364 F116 L118 T119 G124 S125 F148 T150 Y350 T353 E355
BS02 FAD A R266 I273 N276 I279 Q333 I334 G337 R260 I267 N270 I273 Q324 I325 G328
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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