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7FS2

Structure of liver pyruvate kinase in complex with allosteric modulator 13

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004743molecular_functionpyruvate kinase activity
A0006096biological_processglycolytic process
A0030955molecular_functionpotassium ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004743molecular_functionpyruvate kinase activity
B0006096biological_processglycolytic process
B0030955molecular_functionpotassium ion binding
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004743molecular_functionpyruvate kinase activity
C0006096biological_processglycolytic process
C0030955molecular_functionpotassium ion binding
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0004743molecular_functionpyruvate kinase activity
D0006096biological_processglycolytic process
D0030955molecular_functionpotassium ion binding
E0000287molecular_functionmagnesium ion binding
E0003824molecular_functioncatalytic activity
E0004743molecular_functionpyruvate kinase activity
E0006096biological_processglycolytic process
E0030955molecular_functionpotassium ion binding
F0000287molecular_functionmagnesium ion binding
F0003824molecular_functioncatalytic activity
F0004743molecular_functionpyruvate kinase activity
F0006096biological_processglycolytic process
F0030955molecular_functionpotassium ion binding
G0000287molecular_functionmagnesium ion binding
G0003824molecular_functioncatalytic activity
G0004743molecular_functionpyruvate kinase activity
G0006096biological_processglycolytic process
G0030955molecular_functionpotassium ion binding
H0000287molecular_functionmagnesium ion binding
H0003824molecular_functioncatalytic activity
H0004743molecular_functionpyruvate kinase activity
H0006096biological_processglycolytic process
H0030955molecular_functionpotassium ion binding
Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV
ChainResidueDetails
AILE277-VAL289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB
ChainResidueDetails
AARG85
ESER89
FARG85
FSER89
GARG85
GSER89
HARG85
HSER89
ASER89
BARG85
BSER89
CARG85
CSER89
DARG85
DSER89
EARG85

site_idSWS_FT_FI2
Number of Residues96
DetailsBINDING: BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF
ChainResidueDetails
AASN87
ATRP494
AARG501
AARG528
BASN87
BASP125
BTHR126
BLYS282
BGLU284
BGLY307
BASP308
AASP125
BTHR340
BTHR444
BTRP494
BARG501
BARG528
CASN87
CASP125
CTHR126
CLYS282
CGLU284
ATHR126
CGLY307
CASP308
CTHR340
CTHR444
CTRP494
CARG501
CARG528
DASN87
DASP125
DTHR126
ALYS282
DLYS282
DGLU284
DGLY307
DASP308
DTHR340
DTHR444
DTRP494
DARG501
DARG528
EASN87
AGLU284
EASP125
ETHR126
ELYS282
EGLU284
EGLY307
EASP308
ETHR340
ETHR444
ETRP494
EARG501
AGLY307
EARG528
FASN87
FASP125
FTHR126
FLYS282
FGLU284
FGLY307
FASP308
FTHR340
FTHR444
AASP308
FTRP494
FARG501
FARG528
GASN87
GASP125
GTHR126
GLYS282
GGLU284
GGLY307
GASP308
ATHR340
GTHR340
GTHR444
GTRP494
GARG501
GARG528
HASN87
HASP125
HTHR126
HLYS282
HGLU284
ATHR444
HGLY307
HASP308
HTHR340
HTHR444
HTRP494
HARG501
HARG528

site_idSWS_FT_FI3
Number of Residues8
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
ALYS282
BLYS282
CLYS282
DLYS282
ELYS282
FLYS282
GLYS282
HLYS282

site_idSWS_FT_FI4
Number of Residues16
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
AASP12
ESER261
FASP12
FSER261
GASP12
GSER261
HASP12
HSER261
ASER261
BASP12
BSER261
CASP12
CSER261
DASP12
DSER261
EASP12

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PDB entries from 2024-10-30

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