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4JDR

Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0004148molecular_functiondihydrolipoyl dehydrogenase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005960cellular_componentglycine cleavage complex
A0006090biological_processpyruvate metabolic process
A0006099biological_processtricarboxylic acid cycle
A0006103biological_process2-oxoglutarate metabolic process
A0006730biological_processone-carbon metabolic process
A0006979biological_processresponse to oxidative stress
A0008270molecular_functionzinc ion binding
A0015036molecular_functiondisulfide oxidoreductase activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0019464biological_processglycine decarboxylation via glycine cleavage system
A0042802molecular_functionidentical protein binding
A0042867biological_processpyruvate catabolic process
A0045252cellular_componentoxoglutarate dehydrogenase complex
A0045254cellular_componentpyruvate dehydrogenase complex
A0050660molecular_functionflavin adenine dinucleotide binding
B0004148molecular_functiondihydrolipoyl dehydrogenase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005960cellular_componentglycine cleavage complex
B0006090biological_processpyruvate metabolic process
B0006099biological_processtricarboxylic acid cycle
B0006103biological_process2-oxoglutarate metabolic process
B0006730biological_processone-carbon metabolic process
B0006979biological_processresponse to oxidative stress
B0008270molecular_functionzinc ion binding
B0015036molecular_functiondisulfide oxidoreductase activity
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0019464biological_processglycine decarboxylation via glycine cleavage system
B0042802molecular_functionidentical protein binding
B0042867biological_processpyruvate catabolic process
B0045252cellular_componentoxoglutarate dehydrogenase complex
B0045254cellular_componentpyruvate dehydrogenase complex
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues40
DetailsBINDING SITE FOR RESIDUE FAD A 501
ChainResidue
AGLY13
AVAL44
ACYS45
AGLY49
ACYS50
ALYS54
AGLY115
ALEU116
AGLY117
AALA144
AALA145
AALA14
AGLY146
AILE186
AARG273
ALEU280
AGLY312
AASP313
AMET319
ALEU320
AALA321
AHIS322
AGLY15
ATYR352
AHOH601
AHOH616
AHOH639
AHOH648
AHOH649
AHOH650
AHOH779
AHOH828
BHIS445
APRO16
BHOH720
AALA17
AGLU36
AARG37
ATYR38
AGLY43

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES A 502
ChainResidue
AILE185
AILE211
APRO212
AALA213
AGLN317
APRO318
ALEU320
AMES503
ASO4504

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES A 503
ChainResidue
AGLY182
AGLY184
AVAL204
AGLU205
AMET206
AILE271
AMES502
ASO4504
AHOH690

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
AILE185
AILE186
AMES502
AMES503
AHOH664
AHOH690

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
AASP281
AALA282
AGLY283

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 506
ChainResidue
AARG263
AHOH685
AHOH731

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 507
ChainResidue
AASP298
ALYS299

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 508
ChainResidue
ATYR374
AGLU375
ATHR376

site_idAC9
Number of Residues40
DetailsBINDING SITE FOR RESIDUE FAD B 501
ChainResidue
BLEU280
BGLY312
BASP313
BMET319
BLEU320
BALA321
BHIS322
BTYR352
BHOH603
BHOH614
BHOH625
BHOH643
BHOH658
BHOH714
BHOH718
BHOH760
AHIS445
AHOH711
BGLY13
BALA14
BGLY15
BPRO16
BALA17
BGLU36
BARG37
BTYR38
BGLY43
BVAL44
BCYS45
BGLY49
BCYS50
BLYS54
BGLY115
BLEU116
BGLY117
BALA144
BALA145
BGLY146
BILE186
BARG273

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES B 502
ChainResidue
BGLY184
BILE185
BILE186
BPRO212
BALA213
BHOH666
BHOH683
BHOH734
BHOH766

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
BARG263

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 504
ChainResidue
BGLY121
BALA122
BASN123
BTHR124

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGvCLnvGCIP
ChainResidueDetails
AGLY42-PRO52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS445
BHIS445

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU36
BGLU36
BLYS54
BGLY117
BGLY182
BGLU205
BVAL238
BALA270
BASP313
BALA321
ALYS54
AGLY117
AGLY182
AGLU205
AVAL238
AALA270
AASP313
AALA321

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS220
BLYS220

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PDB entries from 2024-07-24

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