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1BUC

THREE-DIMENSIONAL STRUCTURE OF BUTYRYL-COA DEHYDROGENASE FROM MEGASPHAERA ELSDENII

Functional Information from GO Data
ChainGOidnamespacecontents
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0004085molecular_functionbutyryl-CoA dehydrogenase activity
A0006552biological_processL-leucine catabolic process
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0008470molecular_functionisovaleryl-CoA dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
A0050660molecular_functionflavin adenine dinucleotide binding
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0004085molecular_functionbutyryl-CoA dehydrogenase activity
B0006552biological_processL-leucine catabolic process
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0008470molecular_functionisovaleryl-CoA dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE CAA A 384
ChainResidue
ATHR162
AASN182
AHIS183
APHE236
AMET240
AMET241
ALEU243
AASP244
AARG247
ATHR317
ATYR366
AGLU367
AGLY368
AFAD385
ALEU96
APHE126
ATHR129
AGLY134
ATHR135
AALA137
ASER138

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE CAA B 384
ChainResidue
BLEU96
BTHR129
BGLY134
BTHR135
BASN182
BHIS183
BPHE236
BMET240
BMET241
BLEU243
BASP244
BARG247
BTYR366
BGLU367
BGLY368
BFAD385

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FAD A 385
ChainResidue
APHE126
ALEU128
ATHR129
AGLY134
ATHR135
APHE160
ATHR162
AARG272
APHE275
ASER284
AILE285
AGLN340
AILE341
AGLY344
AILE362
AGLU367
ATHR369
AGLU371
AMET375
ACAA384
BGLN283

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD B 385
ChainResidue
AGLN283
BPHE126
BLEU128
BTHR129
BGLY134
BTHR135
BPHE160
BTHR162
BLYS205
BARG272
BGLN274
BPHE275
BLEU279
BPHE282
BSER284
BGLN340
BILE341
BGLY344
BTYR366
BGLU367
BTHR369
BGLU371
BMET375
BCAA384

site_idCA
Number of Residues1
DetailsCATALYTIC BASE, CHAIN A
ChainResidue
AGLU367

site_idCB
Number of Residues1
DetailsCATALYTIC BASE, CHAIN B
ChainResidue
BGLU367

Functional Information from PROSITE/UniProt
site_idPS00072
Number of Residues13
DetailsACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. GLTEpnAGTDasG
ChainResidueDetails
AGLY127-GLY139

site_idPS00073
Number of Residues20
DetailsACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiFGGyGYseEypvaRhmrD
ChainResidueDetails
AGLN340-ASP359

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:8399220
ChainResidueDetails
AGLU367
BGLU367

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PDB entries from 2024-04-24

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