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8CA1

Cryo-EM structure of the ACADVL dimer from Mus musculus.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001659biological_processtemperature homeostasis
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0004466molecular_functionlong-chain fatty acyl-CoA dehydrogenase activity
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0009062biological_processfatty acid catabolic process
A0009409biological_processresponse to cold
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0017099molecular_functionvery-long-chain fatty acyl-CoA dehydrogenase activity
A0030855biological_processepithelial cell differentiation
A0031966cellular_componentmitochondrial membrane
A0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
A0042645cellular_componentmitochondrial nucleoid
A0042802molecular_functionidentical protein binding
A0045717biological_processnegative regulation of fatty acid biosynthetic process
A0046322biological_processnegative regulation of fatty acid oxidation
A0050660molecular_functionflavin adenine dinucleotide binding
A0090181biological_processregulation of cholesterol metabolic process
B0001659biological_processtemperature homeostasis
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0004466molecular_functionlong-chain fatty acyl-CoA dehydrogenase activity
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0009062biological_processfatty acid catabolic process
B0009409biological_processresponse to cold
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0017099molecular_functionvery-long-chain fatty acyl-CoA dehydrogenase activity
B0030855biological_processepithelial cell differentiation
B0031966cellular_componentmitochondrial membrane
B0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
B0042645cellular_componentmitochondrial nucleoid
B0042802molecular_functionidentical protein binding
B0045717biological_processnegative regulation of fatty acid biosynthetic process
B0046322biological_processnegative regulation of fatty acid oxidation
B0050660molecular_functionflavin adenine dinucleotide binding
B0090181biological_processregulation of cholesterol metabolic process
Functional Information from PROSITE/UniProt
site_idPS00072
Number of Residues13
DetailsACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. CLTEpsSGSDvaS
ChainResidueDetails
BCYS216-SER228

site_idPS00073
Number of Residues20
DetailsACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiMGGmGFmkEpgveRvlrD
ChainResidueDetails
BGLN436-ASP455

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P49748
ChainResidueDetails
BGLU463
AGLU463

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P49748
ChainResidueDetails
BPHE215
AGLN563
BTRP250
BPHE462
BALA465
BGLN563
APHE215
ATRP250
APHE462
AALA465

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23576753
ChainResidueDetails
BLYS52
BLYS299
BLYS317
BLYS551
ALYS52
ALYS299
ALYS317
ALYS551

site_idSWS_FT_FI4
Number of Residues16
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
BLYS72
ALYS128
ALYS240
ALYS277
ALYS279
ALYS332
ALYS483
ALYS557
BLYS128
BLYS240
BLYS277
BLYS279
BLYS332
BLYS483
BLYS557
ALYS72

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
BLYS196
BLYS269
BLYS373
BLYS640
ALYS196
ALYS269
ALYS373
ALYS640

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:23281369
ChainResidueDetails
BCYS238
ACYS238

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49748
ChainResidueDetails
BSER518
BSER523
ASER518
ASER523

223790

PDB entries from 2024-08-14

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