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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4P13

Medium chain acyl-CoA dehydrogenase, K304E mutant

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
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
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
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
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
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
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
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006635biological_processfatty acid beta-oxidation
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
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
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006635biological_processfatty acid beta-oxidation
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues30
Detailsbinding site for residue FAD A 401
ChainResidue
ATYR133
AILE374
ATYR375
ATHR378
AGLN380
AHOH548
AHOH555
AHOH558
AHOH561
AHOH566
AHOH579
AVAL135
AHOH656
BARG281
BTHR283
BPHE284
BLEU288
BHIS291
BGLN349
BILE350
BGLY353
BHOH530
ATHR136
DGLN292
AGLY141
ASER142
ATRP166
AILE167
ATHR168
AILE371
site_idAC2
Number of Residues30
Detailsbinding site for residue FAD B 401
ChainResidue
AARG281
ATHR283
APHE284
ALEU288
AHIS291
AGLN349
AILE350
AGLY353
AHOH559
BTYR133
BVAL135
BTHR136
BGLY141
BSER142
BTRP166
BILE167
BTHR168
BILE371
BILE374
BTYR375
BTHR378
BGLN380
BHOH531
BHOH534
BHOH536
BHOH543
BHOH558
BHOH578
BHOH645
CGLN292
site_idAC3
Number of Residues30
Detailsbinding site for residue FAD C 401
ChainResidue
BGLN292
CTYR133
CVAL135
CTHR136
CGLY141
CSER142
CTRP166
CILE167
CTHR168
CILE371
CILE374
CTYR375
CTHR378
CGLN380
CHOH538
CHOH539
CHOH541
CHOH551
CHOH556
CHOH563
CHOH607
DARG281
DTHR283
DPHE284
DLEU288
DHIS291
DGLN349
DILE350
DGLY353
DHOH550
site_idAC4
Number of Residues31
Detailsbinding site for residue FAD D 401
ChainResidue
DTYR133
DVAL135
DTHR136
DGLY141
DSER142
DTRP166
DILE167
DTHR168
DASN214
DILE371
DILE374
DTYR375
DTHR378
DGLN380
DHOH533
DHOH535
DHOH537
DHOH538
DHOH546
DHOH556
DHOH607
DHOH661
AGLN292
CARG281
CTHR283
CPHE284
CLEU288
CHIS291
CGLN349
CILE350
CGLY353
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

246905

PDB entries from 2025-12-31

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