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1PKL

THE STRUCTURE OF LEISHMANIA PYRUVATE KINASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004743molecular_functionpyruvate kinase activity
A0005524molecular_functionATP binding
A0006096biological_processglycolytic process
A0006950biological_processresponse to stress
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0030955molecular_functionpotassium ion binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004743molecular_functionpyruvate kinase activity
B0005524molecular_functionATP binding
B0006096biological_processglycolytic process
B0006950biological_processresponse to stress
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0030955molecular_functionpotassium ion binding
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004743molecular_functionpyruvate kinase activity
C0005524molecular_functionATP binding
C0006096biological_processglycolytic process
C0006950biological_processresponse to stress
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0030955molecular_functionpotassium ion binding
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0004743molecular_functionpyruvate kinase activity
D0005524molecular_functionATP binding
D0006096biological_processglycolytic process
D0006950biological_processresponse to stress
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0030955molecular_functionpotassium ion binding
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0000287molecular_functionmagnesium ion binding
E0003824molecular_functioncatalytic activity
E0004743molecular_functionpyruvate kinase activity
E0005524molecular_functionATP binding
E0006096biological_processglycolytic process
E0006950biological_processresponse to stress
E0016301molecular_functionkinase activity
E0016740molecular_functiontransferase activity
E0030955molecular_functionpotassium ion binding
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0000287molecular_functionmagnesium ion binding
F0003824molecular_functioncatalytic activity
F0004743molecular_functionpyruvate kinase activity
F0005524molecular_functionATP binding
F0006096biological_processglycolytic process
F0006950biological_processresponse to stress
F0016301molecular_functionkinase activity
F0016740molecular_functiontransferase activity
F0030955molecular_functionpotassium ion binding
F0046872molecular_functionmetal ion binding
G0000166molecular_functionnucleotide binding
G0000287molecular_functionmagnesium ion binding
G0003824molecular_functioncatalytic activity
G0004743molecular_functionpyruvate kinase activity
G0005524molecular_functionATP binding
G0006096biological_processglycolytic process
G0006950biological_processresponse to stress
G0016301molecular_functionkinase activity
G0016740molecular_functiontransferase activity
G0030955molecular_functionpotassium ion binding
G0046872molecular_functionmetal ion binding
H0000166molecular_functionnucleotide binding
H0000287molecular_functionmagnesium ion binding
H0003824molecular_functioncatalytic activity
H0004743molecular_functionpyruvate kinase activity
H0005524molecular_functionATP binding
H0006096biological_processglycolytic process
H0006950biological_processresponse to stress
H0016301molecular_functionkinase activity
H0016740molecular_functiontransferase activity
H0030955molecular_functionpotassium ion binding
H0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 3000
ChainResidue
ASER400
AASN401
ATHR402
AARG404
ASER405
AHOH3237

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 3001
ChainResidue
BSER400
BASN401
BTHR402
BGLY403
BARG404
BSER405

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 3002
ChainResidue
CSER400
CASN401
CTHR402
CARG404
CSER405
CALA481

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 3003
ChainResidue
DSER400
DASN401
DTHR402
DGLY403
DARG404
DSER405

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 E 3004
ChainResidue
ESER400
EASN401
ETHR402
EARG404
ESER405
EALA481
EHOH1541

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 F 3005
ChainResidue
FSER400
FASN401
FTHR402
FARG404
FSER405

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 H 3006
ChainResidue
HSER400
HASN401
HTHR402
HGLY403
HARG404
HSER405
HALA481

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 G 3007
ChainResidue
GSER400
GTHR402
GARG404
GSER405
GALA481
GASP482
GHOH2654
GHOH2773
GHOH2900

site_idADP
Number of Residues5
DetailsADP SUBSTRATE BINDING SITE, BY ANALOGY WITH OTHER CRYSTAL STRUCTURES
ChainResidue
AARG49
AASN51
AHIS54
AARG90
AARG174

site_idALL
Number of Residues7
DetailsPUTATIVE ALLOSTERIC EFFECTOR SITE, PARTLY BY ANALOGY WITH OTHER CRYSTAL STRUCTURES
ChainResidue
ASER400
ATHR402
AARG404
ASER405
ALYS453
AARG456
AHIS480

site_idDIV
Number of Residues2
DetailsDIVALENT CATION BINDING SITE, BY ANALOGY WITH OTHER CRYSTAL STRUCTURES
ChainResidue
AGLU240
AASP264

site_idMON
Number of Residues4
DetailsMONOVALENT CATION BINDING SITE, BY ANALOGY WITH OTHER CRYSTAL STRUCTURES
ChainResidue
AASN51
ASER53
AASP83
ATHR84

site_idPEP
Number of Residues4
DetailsPEP SUBSTRATE BINDING SITE, BY ANALOGY WITH OTHER CRYSTAL STRUCTURES
ChainResidue
AARG49
AARG90
ALYS238
ATHR296

Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. ImIICKIENhQGV
ChainResidueDetails
AILE233-VAL245

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
AARG90
ALYS238
AARG49
ATHR296
AGLU332
ASER330

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
BARG90
BLYS238
BARG49
BTHR296
BGLU332
BSER330

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
CARG90
CLYS238
CARG49
CTHR296
CGLU332
CSER330

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
DARG90
DLYS238
DARG49
DTHR296
DGLU332
DSER330

site_idCSA5
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
EARG90
ELYS238
EARG49
ETHR296
EGLU332
ESER330

site_idCSA6
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
FARG90
FLYS238
FARG49
FTHR296
FGLU332
FSER330

site_idCSA7
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
HARG90
HLYS238
HARG49
HTHR296
HGLU332
HSER330

site_idCSA8
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
GARG90
GLYS238
GARG49
GTHR296
GGLU332
GSER330

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PDB entries from 2025-12-24

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