Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3E0V

Crystal structure of pyruvate kinase from Leishmania mexicana in complex with sulphate ions

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
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG49
AASN51
ALYS238

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AGLN297
AGLU300
ASER330
AGLY331
AGLU332

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG174
AHIS54

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 506
ChainResidue
AHIS54
AARG90
AARG175

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 507
ChainResidue
ASER400
AASN401
ATHR402
AGLY403
AARG404
ASER405
AALA481
AASP482

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 508
ChainResidue
ALYS453
AARG456

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 504
ChainResidue
ASER1
AGLN2
BGLN2
BHOH1113

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BARG49
BASN51
BSER53
BLYS238

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 502
ChainResidue
BGLN297
BGLU300
BGLY331
BGLU332

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
BSER53
BHIS54
BARG174
BHOH1100

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 505
ChainResidue
BASN178
BLEU179
BPRO180
BVAL184
BGLU268

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 506
ChainResidue
BHIS54
BARG90
BARG175
BLYS335

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 507
ChainResidue
BSER400
BASN401
BTHR402
BGLY403
BARG404
BSER405
BALA481
BASP482

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 B 508
ChainResidue
BARG456

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 501
ChainResidue
CARG49
CASN51
CLYS238

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 502
ChainResidue
CGLN297
CGLU300
CGLY331
CGLU332

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 503
ChainResidue
CSER53
CHIS54
CGLY55
CARG174

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 505
ChainResidue
CASN178
CLEU179
CVAL184
CARG214
CGLN243
CGLU268

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 506
ChainResidue
CHIS54
CARG90
CARG175

site_idCC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 507
ChainResidue
CSER400
CASN401
CTHR402
CGLY403
CARG404
CSER405
CALA481
CASP482

site_idCC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 508
ChainResidue
CASN401
CARG456

site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 504
ChainResidue
CGLN2
DGLN2
DHOH2149

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 501
ChainResidue
DARG49
DASN51
DSER53
DLYS238

site_idCC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 502
ChainResidue
DGLN297
DGLU300
DSER330
DGLY331
DGLU332

site_idCC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 503
ChainResidue
DHIS54
DGLY55
DHOH2132

site_idCC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 505
ChainResidue
DASN178
DASN241
DGLN243
DGLU268

site_idCC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 506
ChainResidue
DHIS54
DARG90
DARG175
DLYS335

site_idDC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 D 507
ChainResidue
DSER400
DASN401
DTHR402
DGLY403
DARG404
DSER405
DALA481
DASP482

site_idDC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 E 501
ChainResidue
EARG49
EASN51
ELYS238

site_idDC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 E 502
ChainResidue
EGLN297
ESER330
EGLY331
EGLU332

site_idDC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 E 503
ChainResidue
ESER53
EHIS54
EARG174

site_idDC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 E 504
ChainResidue
EGLN2
EHOH3040
EHOH4135
FGLN2

site_idDC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 E 506
ChainResidue
EHIS54
EARG90
EARG175

site_idDC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 E 507
ChainResidue
ESER400
EASN401
ETHR402
EGLY403
EARG404
ESER405
EALA481
EASP482

site_idDC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 F 501
ChainResidue
FARG49
FASN51
FASP83
FLYS238
FSO4506

site_idDC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 F 502
ChainResidue
FGLN297
FGLU300
FGLY331
FGLU332

site_idEC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 F 503
ChainResidue
FSER53
FHIS54
FARG174

site_idEC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 F 506
ChainResidue
FHIS54
FARG90
FARG175
FSO4501

site_idEC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 F 507
ChainResidue
FSER400
FASN401
FTHR402
FGLY403
FARG404
FSER405
FALA481
FASP482

site_idEC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 F 508
ChainResidue
FLYS453
FARG456

site_idEC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 509
ChainResidue
ASER56
DLYS123
DGLU156

site_idEC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 510
ChainResidue
AASN178
ALEU179
ACYS182
AVAL184
AARG214
AGLN243
AGLU268

site_idEC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL E 508
ChainResidue
APHE115
ALYS123
EGLY55
ESER56
EHOH3046
EHOH4110

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 Residues54
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
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

246333

PDB entries from 2025-12-17

PDB statisticsPDBj update infoContact PDBjnumon