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1E0T

R292D mutant of E. coli pyruvate kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004743molecular_functionpyruvate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0008152biological_processmetabolic process
A0009408biological_processresponse to heat
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0030955molecular_functionpotassium ion binding
A0032869biological_processcellular response to insulin stimulus
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A1902912cellular_componentpyruvate kinase complex
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004743molecular_functionpyruvate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006096biological_processglycolytic process
B0008152biological_processmetabolic process
B0009408biological_processresponse to heat
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0030955molecular_functionpotassium ion binding
B0032869biological_processcellular response to insulin stimulus
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B1902912cellular_componentpyruvate kinase complex
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004743molecular_functionpyruvate kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006096biological_processglycolytic process
C0008152biological_processmetabolic process
C0009408biological_processresponse to heat
C0016020cellular_componentmembrane
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0016740molecular_functiontransferase activity
C0030955molecular_functionpotassium ion binding
C0032869biological_processcellular response to insulin stimulus
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C1902912cellular_componentpyruvate kinase complex
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0004743molecular_functionpyruvate kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006096biological_processglycolytic process
D0008152biological_processmetabolic process
D0009408biological_processresponse to heat
D0016020cellular_componentmembrane
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
D0016740molecular_functiontransferase activity
D0030955molecular_functionpotassium ion binding
D0032869biological_processcellular response to insulin stimulus
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D1902912cellular_componentpyruvate kinase complex
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
ATHR378
AGLN379
AGLY380
AGLY381
ALYS382
ASER383
AGLY460

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 702
ChainResidue
BGLY380
BGLY381
BLYS382
BSER383
BSER459
BGLY460
BTHR378
BGLN379

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 703
ChainResidue
CTHR378
CGLN379
CGLY380
CGLY381
CLYS382
CSER459
CGLY460

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 D 704
ChainResidue
DTHR378
DGLN379
DGLY380
DGLY381
DLYS382
DSER383
DSER459
DGLY460
DTHR461

Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IhIISKIENqEGL
ChainResidueDetails
AILE215-LEU227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30613
ChainResidueDetails
AARG32
ATHR278
BARG32
BASN34
BSER36
BASP66
BTHR67
BLYS220
BGLU222
BGLY245
BASP246
AASN34
BTHR278
CARG32
CASN34
CSER36
CASP66
CTHR67
CLYS220
CGLU222
CGLY245
CASP246
ASER36
CTHR278
DARG32
DASN34
DSER36
DASP66
DTHR67
DLYS220
DGLU222
DGLY245
DASP246
AASP66
DTHR278
ATHR67
ALYS220
AGLU222
AGLY245
AASP246

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AARG73
ALYS156
BARG73
BLYS156
CARG73
CLYS156
DARG73
DLYS156

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
ALYS220
BLYS220
CLYS220
DLYS220

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS76
ALYS319
BLYS76
BLYS319
CLYS76
CLYS319
DLYS76
DLYS319

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PDB entries from 2024-04-24

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