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1JEH

CRYSTAL STRUCTURE OF YEAST E3, LIPOAMIDE DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004148molecular_functiondihydrolipoyl dehydrogenase (NADH) activity
A0004375molecular_functionglycine dehydrogenase (decarboxylating) activity
A0004591molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005960cellular_componentglycine cleavage complex
A0006086biological_processpyruvate decarboxylation to acetyl-CoA
A0006099biological_processtricarboxylic acid cycle
A0006103biological_process2-oxoglutarate metabolic process
A0006546biological_processglycine catabolic process
A0006550biological_processL-isoleucine catabolic process
A0006552biological_processL-leucine catabolic process
A0006564biological_processL-serine biosynthetic process
A0006574biological_processL-valine catabolic process
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0042645cellular_componentmitochondrial nucleoid
A0042743biological_processhydrogen peroxide metabolic process
A0045252cellular_componentoxoglutarate dehydrogenase complex
A0045254cellular_componentpyruvate dehydrogenase complex
A0045333biological_processcellular respiration
A0050660molecular_functionflavin adenine dinucleotide binding
B0004148molecular_functiondihydrolipoyl dehydrogenase (NADH) activity
B0004375molecular_functionglycine dehydrogenase (decarboxylating) activity
B0004591molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005960cellular_componentglycine cleavage complex
B0006086biological_processpyruvate decarboxylation to acetyl-CoA
B0006099biological_processtricarboxylic acid cycle
B0006103biological_process2-oxoglutarate metabolic process
B0006546biological_processglycine catabolic process
B0006550biological_processL-isoleucine catabolic process
B0006552biological_processL-leucine catabolic process
B0006564biological_processL-serine biosynthetic process
B0006574biological_processL-valine catabolic process
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0042645cellular_componentmitochondrial nucleoid
B0042743biological_processhydrogen peroxide metabolic process
B0045252cellular_componentoxoglutarate dehydrogenase complex
B0045254cellular_componentpyruvate dehydrogenase complex
B0045333biological_processcellular respiration
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD A 480
ChainResidue
AILE11
AGLY42
ATHR43
ACYS44
AVAL47
AGLY48
ACYS49
ASER52
ALYS53
AGLY118
AALA152
AGLY12
ATHR153
AGLY154
ASER173
AILE194
AARG285
ATYR288
AGLY291
ALEU292
AGLY324
AASP325
AGLY14
AMET331
ALEU332
AALA333
AHIS334
ATYR364
BHIS457
BPRO458
APRO15
AALA16
AVAL34
AGLU35
ALYS36
AARG37

site_idAC2
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD B 580
ChainResidue
AHIS457
APRO458
BILE11
BGLY12
BGLY14
BPRO15
BALA16
BGLU35
BLYS36
BARG37
BGLY42
BTHR43
BCYS44
BGLY48
BCYS49
BSER52
BLYS53
BASN117
BGLY118
BALA152
BTHR153
BGLY154
BSER155
BSER173
BARG285
BTYR288
BALA290
BGLY291
BLEU292
BGLY324
BASP325
BMET331
BLEU332
BALA333
BHIS334
BTYR364
BHOH611

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLnvGCIP
ChainResidueDetails
AGLY41-PRO51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:9538259
ChainResidueDetails
AHIS457
BHIS457

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:9538259, ECO:0000269|Ref.13
ChainResidueDetails
AGLU35
BMET331
ALYS53
AGLY118
AASP325
AMET331
BGLU35
BLYS53
BGLY118
BASP325

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATHR153
BGLY284
AGLY190
AGLU213
AVAL247
AGLY284
BTHR153
BGLY190
BGLU213
BVAL247

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AGLU462
AHIS457

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BGLU462
BHIS457

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS44
ACYS49

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BCYS44
BCYS49

237992

PDB entries from 2025-06-25

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