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1EGC

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

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
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
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
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
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 Residues20
DetailsBINDING SITE FOR RESIDUE CO8 A 400
ChainResidue
ATHR168
AASN191
APHE245
AMET249
APHE252
AASP253
AARG256
ATHR326
ATYR375
AGLY376
AGLY377
AARG388
AFAD399
AHOH2034
BPHE284
AGLU99
ALEU103
AGLY141
ASER142
AVAL144

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE CO8 B 400
ChainResidue
APHE284
BGLU99
BLEU103
BTHR136
BGLY141
BSER142
BVAL144
BALA145
BASN191
BPHE245
BMET249
BPHE252
BASP253
BARG256
BVAL259
BTHR326
BTYR375
BGLY376
BGLY377
BILE381
BFAD399
CASN191
CLYS192

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE CO8 C 400
ChainResidue
BASN191
BLYS192
CGLU99
CGLY100
CLEU103
CTHR136
CSER142
CVAL144
CASN191
CPHE245
CMET249
CPHE252
CASP253
CVAL259
CTHR326
CTYR375
CGLY376
CGLY377
CARG388
CFAD399

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE CO8 D 400
ChainResidue
DGLN95
DTHR96
DLEU103
DGLY141
DSER142
DVAL144
DALA145
DASN191
DPHE245
DMET249
DPHE252
DASP253
DARG256
DARG324
DTHR326
DTYR375
DGLY376
DGLY377
DILE381
DARG388
DFAD399

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD A 399
ChainResidue
ATHR378
AGLN380
ACO8400
BTYR277
BARG281
BTHR283
BLEU288
BHIS291
BILE294
BGLN349
BILE350
BGLY353
DGLN292
ATYR133
AVAL135
ATHR136
AGLY141
ASER142
ATRP166
ATHR168
ATHR222
AILE371
AILE374
ATYR375

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD B 399
ChainResidue
AARG281
ATHR283
APHE284
ALEU288
AHIS291
AILE294
AGLN349
AILE350
AGLY353
BTYR133
BVAL135
BTHR136
BGLY141
BSER142
BTRP166
BTHR168
BTHR222
BILE374
BTYR375
BTHR378
BGLN380
BCO8400
BHOH2050
CGLN292

site_idAC7
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FAD C 399
ChainResidue
BGLN292
CTYR133
CVAL135
CTHR136
CGLY141
CSER142
CTRP166
CILE167
CTHR168
CASN214
CILE374
CTYR375
CTHR378
CGLN380
CCO8400
CHOH2010
DARG281
DTHR283
DLEU288
DHIS291
DILE294
DGLN349
DILE350
DGLY352
DGLY353

site_idAC8
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD D 399
ChainResidue
AGLN292
CARG281
CTHR283
CPHE284
CLEU288
CHIS291
CILE294
CGLN349
CILE350
CGLY353
DTYR133
DVAL135
DTHR136
DGLY141
DSER142
DTRP166
DTHR168
DTHR222
DILE374
DTYR375
DTHR378
DGLN380
DCO8400
DHOH2119

site_idCA1
Number of Residues1
DetailsCATALYTIC BASE IN CHAIN A
ChainResidue
AGLU255

site_idCA2
Number of Residues1
DetailsCATALYTIC BASE IN CHAIN B
ChainResidue
BGLU255

site_idCA3
Number of Residues1
DetailsCATALYTIC BASE IN CHAIN C
ChainResidue
CGLU255

site_idCA4
Number of Residues1
DetailsCATALYTIC BASE IN CHAIN D
ChainResidue
DGLU255

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
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176
ChainResidueDetails
AGLY376
BGLY376
CGLY376
DGLY376

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
ATYR133
DTYR133
DTRP166
DHIS291
ATRP166
AHIS291
BTYR133
BTRP166
BHIS291
CTYR133
CTRP166
CHIS291

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC
ChainResidueDetails
ASER142
CASP253
CARG256
CGLY376
DSER142
DASP253
DARG256
DGLY376
AASP253
AARG256
AGLY376
BSER142
BASP253
BARG256
BGLY376
CSER142

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
AARG281
AGLN349
BARG281
BGLN349
CARG281
CGLN349
DARG281
DGLN349

site_idSWS_FT_FI5
Number of Residues20
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
ChainResidueDetails
ALYS44
BLYS246
CLYS44
CLYS187
CLYS192
CLYS234
CLYS246
DLYS44
DLYS187
DLYS192
DLYS234
ALYS187
DLYS246
ALYS192
ALYS234
ALYS246
BLYS44
BLYS187
BLYS192
BLYS234

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P45952
ChainResidueDetails
ALYS154
BLYS154
CLYS154
DLYS154

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS254
ALYS276
BLYS254
BLYS276
CLYS254
CLYS276
DLYS254
DLYS276

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P45952
ChainResidueDetails
ATHR326
BTHR326
CTHR326
DTHR326

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
AGLU255

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
BGLU255

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
CGLU255

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
DGLU255

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
AGLY376

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
BGLY376

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
CGLY376

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
DGLY376

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PDB entries from 2024-07-17

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