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7Y0B

Crystal structure of human short-chain acyl-CoA dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0004085molecular_functionbutyryl-CoA dehydrogenase activity
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005813cellular_componentcentrosome
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
A0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
A0046359biological_processbutyrate catabolic process
A0050660molecular_functionflavin adenine dinucleotide binding
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0004085molecular_functionbutyryl-CoA dehydrogenase activity
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005813cellular_componentcentrosome
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
B0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
B0046359biological_processbutyrate catabolic process
B0050660molecular_functionflavin adenine dinucleotide binding
C0003995molecular_functionacyl-CoA dehydrogenase activity
C0004085molecular_functionbutyryl-CoA dehydrogenase activity
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0005813cellular_componentcentrosome
C0006631biological_processfatty acid metabolic process
C0006635biological_processfatty acid beta-oxidation
C0016491molecular_functionoxidoreductase activity
C0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
C0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
C0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
C0046359biological_processbutyrate catabolic process
C0050660molecular_functionflavin adenine dinucleotide binding
D0003995molecular_functionacyl-CoA dehydrogenase activity
D0004085molecular_functionbutyryl-CoA dehydrogenase activity
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0005813cellular_componentcentrosome
D0006631biological_processfatty acid metabolic process
D0006635biological_processfatty acid beta-oxidation
D0016491molecular_functionoxidoreductase activity
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
D0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
D0046359biological_processbutyrate catabolic process
D0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PROSITE/UniProt
site_idPS00072
Number of Residues13
DetailsACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. ALSEpgNGSDagA
ChainResidueDetails
AALA153-ALA165

site_idPS00073
Number of Residues20
DetailsACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiLGGmGYvtEmpaeRhyrD
ChainResidueDetails
AGLN365-ASP384

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P15651
ChainResidueDetails
AGLU392
BGLU392
CGLU392
DGLU392

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: in other chain => ECO:0000269|Ref.10
ChainResidueDetails
APHE152
ATRP185
AGLN308
ATHR394
BPHE152
BTRP185
BGLN308
BTHR394
CPHE152
CTRP185
CGLN308
CTHR394
DPHE152
DTRP185
DGLN308
DTHR394

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING:
ChainResidueDetails
ASER161
AASP269
AGLY393
BSER161
BASP269
BGLY393
CSER161
CASP269
CGLY393
DSER161
DASP269
DGLY393

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|Ref.10
ChainResidueDetails
AARG297
AGLN365
BARG297
BGLN365
CARG297
CGLN365
DARG297
DGLN365

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q07417
ChainResidueDetails
ATHR27
BTHR27
CTHR27
DTHR27

site_idSWS_FT_FI6
Number of Residues16
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q07417
ChainResidueDetails
ALYS51
ALYS129
ALYS262
ALYS306
BLYS51
BLYS129
BLYS262
BLYS306
CLYS51
CLYS129
CLYS262
CLYS306
DLYS51
DLYS129
DLYS262
DLYS306

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q07417
ChainResidueDetails
ALYS72
ALYS208
BLYS72
BLYS208
CLYS72
CLYS208
DLYS72
DLYS208

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PDB entries from 2024-06-12

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