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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1EGE

STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE

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
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
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
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
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
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
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD A 399
ChainResidue
ATRP166
ATHR168
AASN214
ATHR222
AILE371
ATHR378
AGLN380
AILE381
BARG281
BTHR283
BPHE284
BLEU288
BHIS291
BILE294
BGLN349
BILE350
BGLY352
BGLY353
DGLN292
ATYR133
AVAL135
ATHR136
AGLY141
ASER142
site_idAC2
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
BILE371
BTYR375
BGLU376
BTHR378
BGLN380
CGLN292
site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD C 399
ChainResidue
BGLN292
CTYR133
CVAL135
CTHR136
CGLY141
CSER142
CTRP166
CTHR168
CTHR222
CILE371
CILE374
CTYR375
CGLU376
CTHR378
CGLN380
DARG281
DTHR283
DPHE284
DLEU288
DHIS291
DILE294
DGLN349
DILE350
DGLY353
site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FAD D 399
ChainResidue
DTHR378
DGLN380
AGLN292
CARG281
CTHR283
CPHE284
CLEU288
CHIS291
CILE294
CGLN349
CILE350
CGLY352
CGLY353
DTYR133
DVAL135
DTHR136
DGLY141
DSER142
DTRP166
DTHR168
DASN214
DTHR222
DILE371
DILE374
DTYR375
DGLU376
site_idCA1
Number of Residues1
DetailsCATALYTIC BASE IN CHAIN A
ChainResidue
AGLU376
site_idCA2
Number of Residues1
DetailsCATALYTIC BASE IN CHAIN B
ChainResidue
BGLU376
site_idCA3
Number of Residues1
DetailsCATALYTIC BASE IN CHAIN C
ChainResidue
CGLU376
site_idCA4
Number of Residues1
DetailsCATALYTIC BASE IN CHAIN D
ChainResidue
DGLU376
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
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
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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