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1ZPD

PYRUVATE DECARBOXYLASE FROM ZYMOMONAS MOBILIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000949biological_processaromatic amino acid family catabolic process to alcohol via Ehrlich pathway
A0003824molecular_functioncatalytic activity
A0004737molecular_functionpyruvate decarboxylase activity
A0005829cellular_componentcytosol
A0016831molecular_functioncarboxy-lyase activity
A0019752biological_processcarboxylic acid metabolic process
A0030976molecular_functionthiamine pyrophosphate binding
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0000949biological_processaromatic amino acid family catabolic process to alcohol via Ehrlich pathway
B0003824molecular_functioncatalytic activity
B0004737molecular_functionpyruvate decarboxylase activity
B0005829cellular_componentcytosol
B0016831molecular_functioncarboxy-lyase activity
B0019752biological_processcarboxylic acid metabolic process
B0030976molecular_functionthiamine pyrophosphate binding
B0046872molecular_functionmetal ion binding
E0000287molecular_functionmagnesium ion binding
E0000949biological_processaromatic amino acid family catabolic process to alcohol via Ehrlich pathway
E0003824molecular_functioncatalytic activity
E0004737molecular_functionpyruvate decarboxylase activity
E0005829cellular_componentcytosol
E0016831molecular_functioncarboxy-lyase activity
E0019752biological_processcarboxylic acid metabolic process
E0030976molecular_functionthiamine pyrophosphate binding
E0046872molecular_functionmetal ion binding
F0000287molecular_functionmagnesium ion binding
F0000949biological_processaromatic amino acid family catabolic process to alcohol via Ehrlich pathway
F0003824molecular_functioncatalytic activity
F0004737molecular_functionpyruvate decarboxylase activity
F0005829cellular_componentcytosol
F0016831molecular_functioncarboxy-lyase activity
F0019752biological_processcarboxylic acid metabolic process
F0030976molecular_functionthiamine pyrophosphate binding
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AASP440
AASN467
AGLY469
ADPX600
AHOH611

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 601
ChainResidue
BHOH611
BASP440
BASN467
BGLY469
BDPX600

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG E 601
ChainResidue
EASP440
EASN467
EGLY469
EDPX600
EHOH611

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F 601
ChainResidue
FASP440
FASN467
FGLY469
FDPX600
FHOH611

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE DPX A 600
ChainResidue
AASP390
AGLY413
AHIS414
AILE415
AGLY439
AASP440
AGLY441
ASER442
AASN467
AGLY469
ATYR470
ATHR471
AILE472
AGLU473
AMG601
AHOH611
AHOH612
AHOH769
AHOH1256
BALA25
BGLY26
BGLU50
BVAL75
BHIS114

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CIT A 610
ChainResidue
AARG310
AARG318
APRO320
ASER321
AHOH709
AHOH746
AHOH789
AHOH1006
AHOH1049
FHIS150
FLYS153
FARG157

site_idAC7
Number of Residues23
DetailsBINDING SITE FOR RESIDUE DPX B 600
ChainResidue
AALA25
AGLY26
AGLU50
AVAL75
AHIS114
BASP390
BGLY413
BHIS414
BILE415
BGLY439
BASP440
BGLY441
BSER442
BASN467
BGLY469
BTYR470
BTHR471
BILE472
BGLU473
BMG601
BHOH611
BHOH612
BHOH842

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CIT B 610
ChainResidue
BARG310
BARG318
BPRO320
BSER321
BHOH688
BHOH782
BHOH819
BHOH861
BHOH1111
EHIS150
ELYS153
EARG157

site_idAC9
Number of Residues23
DetailsBINDING SITE FOR RESIDUE DPX E 600
ChainResidue
EASN467
EGLY469
ETYR470
ETHR471
EILE472
EGLU473
EMG601
EHOH611
EHOH612
EHOH874
FALA25
FGLY26
FGLU50
FVAL75
FHIS114
EASP390
EGLY413
EHIS414
EILE415
EGLY439
EASP440
EGLY441
ESER442

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CIT E 610
ChainResidue
BHIS150
BLYS153
BARG157
EARG310
EARG318
EPRO320
ESER321
EHOH656
EHOH814
EHOH851
EHOH894
EHOH1113

site_idBC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE DPX F 600
ChainResidue
EALA25
EGLY26
EGLU50
EVAL75
EHIS114
FASP390
FGLY413
FHIS414
FILE415
FGLY439
FASP440
FGLY441
FSER442
FASN467
FGLY469
FTYR470
FTHR471
FILE472
FGLU473
FMG601
FHOH611
FHOH612
FHOH943
FHOH1240

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CIT F 610
ChainResidue
AHIS150
ALYS153
AARG157
FARG310
FARG318
FPRO320
FSER321
FHOH712
FHOH793
FHOH885
FHOH920
FHOH962

Functional Information from PROSITE/UniProt
site_idPS00187
Number of Residues20
DetailsTPP_ENZYMES Thiamine pyrophosphate enzymes signature. FGyavgaPerrnIlMvGDGS
ChainResidueDetails
APHE423-SER442

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BASP27
EGLU473
FASP27
FHIS114
FGLU473
AASP27
AHIS114
AGLU473
BHIS114
BGLU473
EASP27
EHIS114

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING:
ChainResidueDetails
BGLU50
BASP440
BASN467
BGLY469
EGLU50
EASP440
EASN467
EGLY469
FGLU50
FASP440
FASN467
FGLY469
AGLU50
AASP440
AASN467
AGLY469

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PDB entries from 2024-06-12

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