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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2A1T

Structure of the human MCAD:ETF E165betaA complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001889biological_processliver development
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005978biological_processglycogen biosynthetic process
A0006082biological_processorganic acid metabolic process
A0006111biological_processregulation of gluconeogenesis
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0007507biological_processheart development
A0009409biological_processresponse to cold
A0009437biological_processcarnitine metabolic process
A0009791biological_processpost-embryonic development
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0019254biological_processcarnitine metabolic process, CoA-linked
A0030424cellular_componentaxon
A0031966cellular_componentmitochondrial membrane
A0033011cellular_componentperinuclear theca
A0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
A0042594biological_processresponse to starvation
A0042802molecular_functionidentical protein binding
A0045329biological_processcarnitine biosynthetic process
A0050660molecular_functionflavin adenine dinucleotide binding
A0051791biological_processmedium-chain fatty acid metabolic process
A0051793biological_processmedium-chain fatty acid catabolic process
A0055007biological_processcardiac muscle cell differentiation
A0070991molecular_functionmedium-chain fatty acyl-CoA dehydrogenase activity
A0097228cellular_componentsperm principal piece
A0120238cellular_componentsperm glycocalyx
B0001889biological_processliver development
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005978biological_processglycogen biosynthetic process
B0006082biological_processorganic acid metabolic process
B0006111biological_processregulation of gluconeogenesis
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0007507biological_processheart development
B0009409biological_processresponse to cold
B0009437biological_processcarnitine metabolic process
B0009791biological_processpost-embryonic development
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0019254biological_processcarnitine metabolic process, CoA-linked
B0030424cellular_componentaxon
B0031966cellular_componentmitochondrial membrane
B0033011cellular_componentperinuclear theca
B0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
B0042594biological_processresponse to starvation
B0042802molecular_functionidentical protein binding
B0045329biological_processcarnitine biosynthetic process
B0050660molecular_functionflavin adenine dinucleotide binding
B0051791biological_processmedium-chain fatty acid metabolic process
B0051793biological_processmedium-chain fatty acid catabolic process
B0055007biological_processcardiac muscle cell differentiation
B0070991molecular_functionmedium-chain fatty acyl-CoA dehydrogenase activity
B0097228cellular_componentsperm principal piece
B0120238cellular_componentsperm glycocalyx
C0001889biological_processliver development
C0003995molecular_functionacyl-CoA dehydrogenase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0005978biological_processglycogen biosynthetic process
C0006082biological_processorganic acid metabolic process
C0006111biological_processregulation of gluconeogenesis
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006635biological_processfatty acid beta-oxidation
C0007507biological_processheart development
C0009409biological_processresponse to cold
C0009437biological_processcarnitine metabolic process
C0009791biological_processpost-embryonic development
C0016491molecular_functionoxidoreductase activity
C0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
C0019254biological_processcarnitine metabolic process, CoA-linked
C0030424cellular_componentaxon
C0031966cellular_componentmitochondrial membrane
C0033011cellular_componentperinuclear theca
C0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
C0042594biological_processresponse to starvation
C0042802molecular_functionidentical protein binding
C0045329biological_processcarnitine biosynthetic process
C0050660molecular_functionflavin adenine dinucleotide binding
C0051791biological_processmedium-chain fatty acid metabolic process
C0051793biological_processmedium-chain fatty acid catabolic process
C0055007biological_processcardiac muscle cell differentiation
C0070991molecular_functionmedium-chain fatty acyl-CoA dehydrogenase activity
C0097228cellular_componentsperm principal piece
C0120238cellular_componentsperm glycocalyx
D0001889biological_processliver development
D0003995molecular_functionacyl-CoA dehydrogenase activity
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0005978biological_processglycogen biosynthetic process
D0006082biological_processorganic acid metabolic process
D0006111biological_processregulation of gluconeogenesis
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006635biological_processfatty acid beta-oxidation
D0007507biological_processheart development
D0009409biological_processresponse to cold
D0009437biological_processcarnitine metabolic process
D0009791biological_processpost-embryonic development
D0016491molecular_functionoxidoreductase activity
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0019254biological_processcarnitine metabolic process, CoA-linked
D0030424cellular_componentaxon
D0031966cellular_componentmitochondrial membrane
D0033011cellular_componentperinuclear theca
D0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
D0042594biological_processresponse to starvation
D0042802molecular_functionidentical protein binding
D0045329biological_processcarnitine biosynthetic process
D0050660molecular_functionflavin adenine dinucleotide binding
D0051791biological_processmedium-chain fatty acid metabolic process
D0051793biological_processmedium-chain fatty acid catabolic process
D0055007biological_processcardiac muscle cell differentiation
D0070991molecular_functionmedium-chain fatty acyl-CoA dehydrogenase activity
D0097228cellular_componentsperm principal piece
D0120238cellular_componentsperm glycocalyx
R0005515molecular_functionprotein binding
R0005739cellular_componentmitochondrion
R0005759cellular_componentmitochondrial matrix
R0009055molecular_functionelectron transfer activity
R0009063biological_processamino acid catabolic process
R0016491molecular_functionoxidoreductase activity
R0022904biological_processrespiratory electron transport chain
R0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
R0045251cellular_componentelectron transfer flavoprotein complex
R0050660molecular_functionflavin adenine dinucleotide binding
S0005515molecular_functionprotein binding
S0005739cellular_componentmitochondrion
S0005759cellular_componentmitochondrial matrix
S0009055molecular_functionelectron transfer activity
S0009063biological_processamino acid catabolic process
S0022904biological_processrespiratory electron transport chain
S0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
S0045251cellular_componentelectron transfer flavoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE AMP S 600
ChainResidue
SALA9
SALA126
SASP129
SCYS131
SASN132
SGLN133
STHR134
SVAL10
SLYS11
SASN39
SCYS42
SCYS66
SLEU122
SGLY123
SGLN125
site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FAD A 399
ChainResidue
ATYR133
AVAL135
ATHR136
AGLY141
ASER142
ATRP166
AILE167
ATHR168
AILE371
AILE374
ATYR375
AGLU376
ATHR378
AGLN380
ALEU384
AHOH412
BARG281
BTHR283
BPHE284
BLEU288
BHIS291
BGLN349
BILE350
BGLY353
DGLN292
site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FAD B 1399
ChainResidue
AARG281
ATHR283
APHE284
ALEU288
AHIS291
AILE294
AGLN349
AILE350
AGLY353
BTYR133
BVAL135
BTHR136
BGLY141
BSER142
BTRP166
BTHR168
BILE371
BTYR375
BTHR378
BGLN380
CGLN292
site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FAD C 2399
ChainResidue
BGLN292
CTYR133
CVAL135
CTHR136
CGLY141
CSER142
CTRP166
CILE167
CTHR168
CASN214
CILE371
CILE374
CTHR378
CGLN380
DARG281
DTHR283
DPHE284
DLEU288
DHIS291
DGLN349
DILE350
DGLY353
site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD D 3399
ChainResidue
DTHR168
DILE371
DILE374
DTYR375
DTHR378
DGLN380
DHOH3402
AGLN292
CARG281
CTHR283
CPHE284
CLEU288
CHIS291
CILE294
CGLN349
CILE350
CGLY353
DTYR133
DVAL135
DTHR136
DGLY141
DSER142
DTRP166
site_idAC6
Number of Residues30
DetailsBINDING SITE FOR RESIDUE FAD R 599
ChainResidue
CGLN163
CMET165
DASN357
RGLY222
RARG223
RGLY224
RLYS226
RSER248
RARG249
RALA250
RGLN262
RVAL263
RGLY264
RGLN265
RTHR266
RGLY267
RGLY279
RILE280
RSER281
RALA283
RGLN285
RHIS286
RASN300
RLYS301
RASP302
RALA317
RASP318
RLEU319
RPHE320
RHOH602
Functional Information from PROSITE/UniProt
site_idPS00072
Number of Residues13
DetailsACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. CVTEpgAGSDvaG
ChainResidueDetails
ACYS134-GLY146
site_idPS00073
Number of Residues20
DetailsACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiLGGnGFntEypveKlmrD
ChainResidueDetails
AGLN349-ASP368
site_idPS00696
Number of Residues27
DetailsETF_ALPHA Electron transfer flavoprotein alpha-subunit signature. LYIAvGISGaIQHlaGmkdsktIvAIN
ChainResidueDetails
RLEU274-ASN300
site_idPS01065
Number of Residues21
DetailsETF_BETA Electron transfer flavoprotein beta-subunit signature. VeRaiDGGl.EtLrlklPaVVT
ChainResidueDetails
SVAL162-THR182
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"1970566","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8823176","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues64
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"15159392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15975918","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8823176","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2014","submissionDatabase":"PDB data bank","title":"Medium chain acyl-CoA dehydrogenase, K304E mutant.","authors":["Battaile K.P.","Mohsen A.-W.","Vockley J."]}},{"source":"PDB","id":"1EGC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EGD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EGE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T9G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A1T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4P13","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8823176","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EGC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15159392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15975918","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8823176","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2014","submissionDatabase":"PDB data bank","title":"Medium chain acyl-CoA dehydrogenase, K304E mutant.","authors":["Battaile K.P.","Mohsen A.-W.","Vockley J."]}},{"source":"PDB","id":"1EGC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EGD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EGE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T9G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A1T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4P13","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues20
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P45952","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P45952","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P45952","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues184
DetailsRegion: {"description":"Domain I","evidences":[{"source":"PubMed","id":"8962055","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15975918","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8962055","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A1T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues7
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99LC5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues5
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99LC5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q99LC5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99LC5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues22
DetailsRegion: {"description":"Recognition loop","evidences":[{"source":"PubMed","id":"15159392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25023281","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15159392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15975918","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8962055","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T9G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A1T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine; by ETFBKMT","evidences":[{"source":"PubMed","id":"25023281","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25416781","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DCW4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
ATHR255
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
BTHR255
site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
CTHR255
site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
DTHR255
site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
AGLU376
site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
BGLU376
site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
CGLU376
site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
DGLU376

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PDB entries from 2025-10-08

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