Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8SGP

human liver mitochondrial Medium-chain specific 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
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
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
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
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
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
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
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
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
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
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
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
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 PROSITE/UniProt
site_idPS00072
Number of Residues13
DetailsACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. CVTEpgAGSDvaG
ChainResidueDetails
ACYS159-GLY171

site_idPS00073
Number of Residues20
DetailsACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiLGGnGFntEypveKlmrD
ChainResidueDetails
AGLN374-ASP393

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176
ChainResidueDetails
AGLU401
BGLU401
CGLU401
DGLU401

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13
ChainResidueDetails
ATYR158
ATRP191
AHIS316
BTYR158
BTRP191
BHIS316
CTYR158
CTRP191
CHIS316
DTYR158
DTRP191
DHIS316

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC
ChainResidueDetails
ASER167
AASP278
AARG281
AGLU401
BSER167
BASP278
BARG281
BGLU401
CSER167
CASP278
CARG281
CGLU401
DSER167
DASP278
DARG281
DGLU401

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13
ChainResidueDetails
AARG306
AGLN374
BARG306
BGLN374
CARG306
CGLN374
DARG306
DGLN374

site_idSWS_FT_FI5
Number of Residues20
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
ChainResidueDetails
ALYS69
ALYS212
ALYS217
ALYS259
ALYS271
BLYS69
BLYS212
BLYS217
BLYS259
BLYS271
CLYS69
CLYS212
CLYS217
CLYS259
CLYS271
DLYS69
DLYS212
DLYS217
DLYS259
DLYS271

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P45952
ChainResidueDetails
ALYS179
BLYS179
CLYS179
DLYS179

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS279
ALYS301
BLYS279
BLYS301
CLYS279
CLYS301
DLYS279
DLYS301

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P45952
ChainResidueDetails
ATHR351
BTHR351
CTHR351
DTHR351

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon