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1QPB

PYRUVATE DECARBOYXLASE FROM YEAST (FORM B) COMPLEXED WITH PYRUVAMIDE

Replaces:  1YPD
Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000949biological_processaromatic amino acid family catabolic process to alcohol via Ehrlich pathway
A0000955biological_processamino acid catabolic process via Ehrlich pathway
A0003824molecular_functioncatalytic activity
A0004737molecular_functionpyruvate decarboxylase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006090biological_processpyruvate metabolic process
A0006559biological_processL-phenylalanine catabolic process
A0006569biological_processtryptophan catabolic process
A0009083biological_processbranched-chain amino acid catabolic process
A0016831molecular_functioncarboxy-lyase activity
A0019655biological_processglycolytic fermentation to ethanol
A0030976molecular_functionthiamine pyrophosphate binding
A0046872molecular_functionmetal ion binding
A0047433molecular_functionbranched-chain-2-oxoacid decarboxylase activity
A0047434molecular_functionindolepyruvate decarboxylase activity
A0050177molecular_functionphenylpyruvate decarboxylase activity
B0000287molecular_functionmagnesium ion binding
B0000949biological_processaromatic amino acid family catabolic process to alcohol via Ehrlich pathway
B0000955biological_processamino acid catabolic process via Ehrlich pathway
B0003824molecular_functioncatalytic activity
B0004737molecular_functionpyruvate decarboxylase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006090biological_processpyruvate metabolic process
B0006559biological_processL-phenylalanine catabolic process
B0006569biological_processtryptophan catabolic process
B0009083biological_processbranched-chain amino acid catabolic process
B0016831molecular_functioncarboxy-lyase activity
B0019655biological_processglycolytic fermentation to ethanol
B0030976molecular_functionthiamine pyrophosphate binding
B0046872molecular_functionmetal ion binding
B0047433molecular_functionbranched-chain-2-oxoacid decarboxylase activity
B0047434molecular_functionindolepyruvate decarboxylase activity
B0050177molecular_functionphenylpyruvate decarboxylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AASP444
AASN471
AGLY473
ATPP600
AHOH2077

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 601
ChainResidue
BTPP600
BHOH2043
BASP444
BASN471
BGLY473
BTHR475

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE TPP A 600
ChainResidue
ATHR390
AGLY413
AILE415
AGLY443
AASP444
AGLY445
ASER446
AASN471
AGLY473
ATYR474
ATHR475
AILE476
AGLU477
AMG601
AHOH2077
AHOH2084
BPRO26
BGLU51
BVAL76
BPYM602

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE TPP B 600
ChainResidue
APRO26
AGLU51
AVAL76
BGLY389
BTHR390
BGLY413
BSER414
BILE415
BGLY443
BASP444
BGLY445
BSER446
BASN471
BGLY473
BTYR474
BTHR475
BILE476
BMG601
BHOH2043

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYM B 602
ChainResidue
AGLU477
ATPP600
AHOH2085
BASP28
BHIS114
BHIS115

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PYM A 602
ChainResidue
ATYR157
AVAL158
AARG224
AHIS225
AASP226

Functional Information from PROSITE/UniProt
site_idPS00187
Number of Residues20
DetailsTPP_ENZYMES Thiamine pyrophosphate enzymes signature. FAaeeidPkkrvIlFiGDGS
ChainResidueDetails
APHE427-SER446

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:10651824
ChainResidueDetails
AASP28
ATYR157
AGLU477
BASP28
BTYR157
BGLU477

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:10651824, ECO:0007744|PDB:1QPB
ChainResidueDetails
AHIS115
AARG224
BHIS115
BARG224

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:10651824, ECO:0007744|PDB:1QPB
ChainResidueDetails
ATHR390
BGLY445
BASN471
BGLY473
AGLY413
AASP444
AGLY445
AASN471
AGLY473
BTHR390
BGLY413
BASP444

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:10545125, ECO:0000269|PubMed:9298649
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000269|PubMed:26046779
ChainResidueDetails
AARG161
BARG161

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER223
BSER223

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ATHR266
BTHR266

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
AALA336
ATHR522
BALA336
BTHR522

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR353
BTHR353

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER526
BSER526

site_idSWS_FT_FI11
Number of Residues16
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS212
BLYS233
BLYS269
BLYS332
BLYS484
BLYS505
BLYS520
ALYS233
ALYS269
ALYS332
ALYS484
ALYS505
ALYS520
BLYS212

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pvd
ChainResidueDetails
AASP28
AHIS114
AHIS115
AGLU477

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pvd
ChainResidueDetails
BASP28
BHIS114
BHIS115
BGLU477

site_idMCSA1
Number of Residues9
DetailsM-CSA 215
ChainResidueDetails
AASP28hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AGLU51hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS114activator, electrostatic stabiliser, hydrogen bond donor, polar interaction
AHIS115electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor
AGLY413activator, electrostatic stabiliser, hydrogen bond acceptor
AASP444metal ligand
AASN471metal ligand
AGLY473metal ligand
AGLU477electrostatic stabiliser, polar interaction

site_idMCSA2
Number of Residues9
DetailsM-CSA 215
ChainResidueDetails
BASP28hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
BGLU51hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS114activator, electrostatic stabiliser, hydrogen bond donor, polar interaction
BHIS115electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor
BGLY413activator, electrostatic stabiliser, hydrogen bond acceptor
BASP444metal ligand
BASN471metal ligand
BGLY473metal ligand
BGLU477electrostatic stabiliser, polar interaction

223790

PDB entries from 2024-08-14

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