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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1T9G

Structure of the human MCAD:ETF complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005978biological_processglycogen biosynthetic process
A0006111biological_processregulation of gluconeogenesis
A0006635biological_processfatty acid beta-oxidation
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0019254biological_processcarnitine metabolic process, CoA-linked
A0030424cellular_componentaxon
A0031966cellular_componentmitochondrial membrane
A0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
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
A0070991molecular_functionmedium-chain fatty acyl-CoA dehydrogenase activity
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005978biological_processglycogen biosynthetic process
B0006111biological_processregulation of gluconeogenesis
B0006635biological_processfatty acid beta-oxidation
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0019254biological_processcarnitine metabolic process, CoA-linked
B0030424cellular_componentaxon
B0031966cellular_componentmitochondrial membrane
B0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
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
B0070991molecular_functionmedium-chain fatty acyl-CoA dehydrogenase activity
C0003995molecular_functionacyl-CoA dehydrogenase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0005978biological_processglycogen biosynthetic process
C0006111biological_processregulation of gluconeogenesis
C0006635biological_processfatty acid beta-oxidation
C0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
C0019254biological_processcarnitine metabolic process, CoA-linked
C0030424cellular_componentaxon
C0031966cellular_componentmitochondrial membrane
C0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
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
C0070991molecular_functionmedium-chain fatty acyl-CoA dehydrogenase activity
D0003995molecular_functionacyl-CoA dehydrogenase activity
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0005978biological_processglycogen biosynthetic process
D0006111biological_processregulation of gluconeogenesis
D0006635biological_processfatty acid beta-oxidation
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0019254biological_processcarnitine metabolic process, CoA-linked
D0030424cellular_componentaxon
D0031966cellular_componentmitochondrial membrane
D0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
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
D0070991molecular_functionmedium-chain fatty acyl-CoA dehydrogenase activity
R0005515molecular_functionprotein binding
R0005739cellular_componentmitochondrion
R0005759cellular_componentmitochondrial matrix
R0009055molecular_functionelectron transfer activity
R0009063biological_processamino acid catabolic process
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 Residues14
DetailsBINDING SITE FOR RESIDUE AMP S 600
ChainResidue
SALA9
SASP129
SCYS131
SASN132
SGLN133
STHR134
SVAL10
SLYS11
SCYS42
SCYS66
SLEU122
SGLY123
SGLN125
SALA126
site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD A 399
ChainResidue
ATYR133
ACYS134
AVAL135
ATHR136
AGLY141
ASER142
ATRP166
AILE167
ATHR168
AILE371
AILE374
ATYR375
AGLU376
ATHR378
AGLN380
BARG281
BTHR283
BPHE284
BHIS291
BGLN349
BILE350
BGLY353
DGLN292
site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD B 399
ChainResidue
AARG281
ATHR283
APHE284
ALEU288
AHIS291
AGLN349
AILE350
AGLY353
BTYR133
BVAL135
BTHR136
BGLY141
BSER142
BTRP166
BILE167
BTHR168
BASN214
BTHR222
BILE374
BTYR375
BTHR378
BGLN380
CGLN292
site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD C 399
ChainResidue
BGLN292
CTYR133
CVAL135
CTHR136
CGLY141
CSER142
CTRP166
CILE167
CTHR168
CILE371
CILE374
CTYR375
CTHR378
CGLN380
DARG281
DTHR283
DPHE284
DLEU288
DHIS291
DGLN349
DILE350
DGLY352
DGLY353
site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD D 399
ChainResidue
DASN214
DILE371
DILE374
DTYR375
DGLU376
DTHR378
DGLN380
AGLN292
CARG281
CTHR283
CPHE284
CLEU288
CHIS291
CGLN349
CILE350
CGLY353
DTYR133
DVAL135
DTHR136
DGLY141
DSER142
DTRP166
DTHR168
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. VeReiDGGl.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 Residues5
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99LC5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues5
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99LC5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q99LC5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99LC5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
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_FI15
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_FI16
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
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_FI18
Number of Residues1
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 2026-04-01

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