Structure of PDB 5ez3 Chain A

Receptor sequence
>5ez3A (length=540) Species: 224914 (Brucella melitensis bv. 1 str. 16M) [Search protein sequence]
KTHEVTNQTPPITGTNAYLGDPLLMQIAARFPKELHTELEQAGRFVLSAE
AQDLARLANTELPKLRTHDRQGRRIDLVEYHPAYHALMRRSVAQGLHSSI
WEDNPLESGRRHQARAARFYLTAQLEAGHLCPLTMTSASLAALMASPEVY
KQWSPAVLSRKYDFSQKPAFRKQGVTLGMGMTEKQGGTDVRANATRAEPA
IGGAWRLTGHKWFMSAPMSDAFLTLAQTKEGLSCFLLPRLGEKGESNGFF
FQRLKDKLGNRSNASSEVEFDGALGQMIGSPGEGVKTIMDMVTLTRLDCA
VASAGLMRSGLAEAVHHSRHRHVFGKPLVEQPLMQRVLADMALDVAGATA
LSMRLARAFDMAASDRAEAAFARSMTPVVKYWVCKIAPALLYEAMECLGG
NGYIEDGNLARAYREAPVNAIWEGSGNVMALDVARVLSRAPALFDGVLDW
ISGQLGPRGQGTIDVLRAALQLTETDQGVARLLTEQLAFAAAAAELRQLG
ADDIADAFIETRLGGLWRTTYGMLDARHNAMRIIDQLYPA
3D structure
PDB5ez3 Crystal structure Acyl-CoA dehydrogenase from Brucella melitensis in complex with FAD
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M192 T193 T306 E434 R446
Catalytic site (residue number reindexed from 1) M181 T182 T295 E423 R435
Enzyme Commision number 1.3.8.-
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 M192 T193 G197 G198 T199 F224 S226 W433 E434 S436 N438 L442 M181 T182 G186 G187 T188 F213 S215 W422 E423 S425 N427 L431
BS02 FAD A R332 F335 L339 Q342 M345 E407 C408 G411 R321 F324 L328 Q331 M334 E396 C397 G400
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

View graph for
Molecular Function
External links
PDB RCSB:5ez3, PDBe:5ez3, PDBj:5ez3
PDBsum5ez3
PubMed
UniProtQ8YC61

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