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2VGI

HUMAN ERYTHROCYTE PYRUVATE KINASE: R486W MUTANT

Replaces:  1LIX
Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001666biological_processresponse to hypoxia
A0003824molecular_functioncatalytic activity
A0004743molecular_functionpyruvate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0007584biological_processresponse to nutrient
A0009749biological_processresponse to glucose
A0010038biological_processresponse to metal ion
A0016301molecular_functionkinase activity
A0030955molecular_functionpotassium ion binding
A0032869biological_processcellular response to insulin stimulus
A0033198biological_processresponse to ATP
A0042866biological_processpyruvate biosynthetic process
A0046872molecular_functionmetal ion binding
A0048029molecular_functionmonosaccharide binding
A0051591biological_processresponse to cAMP
A0070062cellular_componentextracellular exosome
A0071872biological_processcellular response to epinephrine stimulus
B0000287molecular_functionmagnesium ion binding
B0001666biological_processresponse to hypoxia
B0003824molecular_functioncatalytic activity
B0004743molecular_functionpyruvate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006096biological_processglycolytic process
B0007584biological_processresponse to nutrient
B0009749biological_processresponse to glucose
B0010038biological_processresponse to metal ion
B0016301molecular_functionkinase activity
B0030955molecular_functionpotassium ion binding
B0032869biological_processcellular response to insulin stimulus
B0033198biological_processresponse to ATP
B0042866biological_processpyruvate biosynthetic process
B0046872molecular_functionmetal ion binding
B0048029molecular_functionmonosaccharide binding
B0051591biological_processresponse to cAMP
B0070062cellular_componentextracellular exosome
B0071872biological_processcellular response to epinephrine stimulus
C0000287molecular_functionmagnesium ion binding
C0001666biological_processresponse to hypoxia
C0003824molecular_functioncatalytic activity
C0004743molecular_functionpyruvate kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006096biological_processglycolytic process
C0007584biological_processresponse to nutrient
C0009749biological_processresponse to glucose
C0010038biological_processresponse to metal ion
C0016301molecular_functionkinase activity
C0030955molecular_functionpotassium ion binding
C0032869biological_processcellular response to insulin stimulus
C0033198biological_processresponse to ATP
C0042866biological_processpyruvate biosynthetic process
C0046872molecular_functionmetal ion binding
C0048029molecular_functionmonosaccharide binding
C0051591biological_processresponse to cAMP
C0070062cellular_componentextracellular exosome
C0071872biological_processcellular response to epinephrine stimulus
D0000287molecular_functionmagnesium ion binding
D0001666biological_processresponse to hypoxia
D0003824molecular_functioncatalytic activity
D0004743molecular_functionpyruvate kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006096biological_processglycolytic process
D0007584biological_processresponse to nutrient
D0009749biological_processresponse to glucose
D0010038biological_processresponse to metal ion
D0016301molecular_functionkinase activity
D0030955molecular_functionpotassium ion binding
D0032869biological_processcellular response to insulin stimulus
D0033198biological_processresponse to ATP
D0042866biological_processpyruvate biosynthetic process
D0046872molecular_functionmetal ion binding
D0048029molecular_functionmonosaccharide binding
D0051591biological_processresponse to cAMP
D0070062cellular_componentextracellular exosome
D0071872biological_processcellular response to epinephrine stimulus
Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV
ChainResidueDetails
AILE308-VAL320

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB
ChainResidueDetails
AARG116
ASER120
BARG116
BSER120
CARG116
CSER120
DARG116
DSER120

site_idSWS_FT_FI2
Number of Residues48
DetailsBINDING: BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
ChainResidueDetails
AASN118
ATRP525
AARG532
AARG559
BASN118
BASP156
BTHR157
BLYS313
BGLU315
BGLY338
BASP339
AASP156
BTHR371
BTHR475
BTRP525
BARG532
BARG559
CASN118
CASP156
CTHR157
CLYS313
CGLU315
ATHR157
CGLY338
CASP339
CTHR371
CTHR475
CTRP525
CARG532
CARG559
DASN118
DASP156
DTHR157
ALYS313
DLYS313
DGLU315
DGLY338
DASP339
DTHR371
DTHR475
DTRP525
DARG532
DARG559
AGLU315
AGLY338
AASP339
ATHR371
ATHR475

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AARG163
ALYS250
BARG163
BLYS250
CARG163
CLYS250
DARG163
DLYS250

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
ALYS313
BLYS313
CLYS313
DLYS313

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER292
BSER292
CSER292
DSER292

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
ALYS313
AGLU407
AARG116
ATHR371
AARG163
ASER405

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
BLYS313
BGLU407
BARG116
BTHR371
BARG163
BSER405

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
CLYS313
CGLU407
CARG116
CTHR371
CARG163
CSER405

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
DLYS313
DGLU407
DARG116
DTHR371
DARG163
DSER405

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PDB entries from 2024-07-10

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