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1L8A

E. COLI PYRUVATE DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004738molecular_functionpyruvate dehydrogenase activity
A0004739molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0030976molecular_functionthiamine pyrophosphate binding
A0036094molecular_functionsmall molecule binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042867biological_processpyruvate catabolic process
A0045254cellular_componentpyruvate dehydrogenase complex
A0046872molecular_functionmetal ion binding
A0060090molecular_functionmolecular adaptor activity
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004738molecular_functionpyruvate dehydrogenase activity
B0004739molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0030976molecular_functionthiamine pyrophosphate binding
B0036094molecular_functionsmall molecule binding
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042867biological_processpyruvate catabolic process
B0045254cellular_componentpyruvate dehydrogenase complex
B0046872molecular_functionmetal ion binding
B0060090molecular_functionmolecular adaptor activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 888
ChainResidue
ATPP887
BASP230
BASN260
BGLN262
BHOH903

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 888
ChainResidue
BTPP887
AASP230
AASN260
AGLN262
AHOH909

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE TPP A 887
ChainResidue
AASP521
AGLU522
AILE569
AGLU571
APHE602
AARG606
AMG888
AHOH901
AHOH972
AHOH1041
BSER109
BGLN140
BHIS142
BVAL192
BMET194
BGLY229
BASP230
BGLY231
BGLU232
BGLU235
BASN260
BGLN262
BARG263
BLEU264
BLYS392
BHOH903

site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE TPP B 887
ChainResidue
ASER109
AGLN140
AHIS142
AVAL192
AMET194
AGLY229
AASP230
AGLY231
AGLU232
AGLU235
AASN260
AGLN262
AARG263
ALEU264
ALYS392
AHOH909
BASP521
BGLU522
BILE569
BGLU571
BPHE602
BARG606
BMG888
BHOH907
BHOH971
BHOH1240

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AGLY231
ALEU261
AARG263
BGLY231
BLEU261
BARG263

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALEU716
BLEU716

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
AHIS646
AGLU571

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BHIS646
BGLU571

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
AGLU571

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BGLU571

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
AHIS106
AHIS336

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BHIS106
BHIS336

219140

PDB entries from 2024-05-01

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