Structure of PDB 5ez3 Chain C

Receptor sequence

>5ez3C (length=541) Species: 224914 (Brucella melitensis bv. 1 str. 16M)

KTHEVTNQTPPITGTNAYLGDPLLMQIAARFPKELHTELEQAGRFVLSAE
AQDLARLANTELPKLRTHDRQGRRIDLVEYHPAYHALMRRSVAQGLHSSI
WEDNPLESGRRHQARAARFYLTAQLEAGHLCPLTMTSASLAALMASPEVY
KQWSPAVLSRKYDFSQKPAFRKQGVTLGMGMTEKQGGTDVRANATRAEPA
IGGAWRLTGHKWFMSAPMSDAFLTLAQTKEGLSCFLLPRLGEKGESNGFF
FQRLKDKLGNRSNASSEVEFDGALGQMIGSPGEGVKTIMDMVTLTRLDCA
VASAGLMRSGLAEAVHHSRHRHVFGKPLVEQPLMQRVLADMALDVAGATA
LSMRLARAFDMAASDRAEAAFARSMTPVVKYWVCKIAPALLYEAMECLGG
NGYIEDGNLARAYREAPVNAIWEGSGNVMALDVARVLSRAPALFDGVLDW
ISGQLGPRGQGTIDVLRAALQLTETDQGVARLLTEQLAFAAAAAELRQLG
ADDIADAFIETRLGGLWRTTYGMLDARHNAMRIIDQLYPAS

3D structure

• PDB: 5ez3 Crystal structure Acyl-CoA dehydrogenase from Brucella melitensis in complex with FAD
• Chain: C
• Resolution: 2.15 Å

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	C	M190 M192 T193 G197 G198 T199 F224 S226 W433 E434 S436 N438 L442	M179 M181 T182 G186 G187 T188 F213 S215 W422 E423 S425 N427 L431
BS02	FAD	C	R332 F335 L339 Q342 M345 E407 C408 G410 G411	R321 F324 L328 Q331 M334 E396 C397 G399 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

External links

• PDB: RCSB:5ez3, PDBe:5ez3, PDBj:5ez3
• PDBsum: 5ez3
• UniProt: Q8YC61