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3QV8

Crystal structure of Leishmania mexicana pyruvate kinase(LmPYK)in complex with benzothiazole-2,5-disulfonic acid.

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
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
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE S62 D 499
ChainResidue
DTHR26
DPRO29
DARG49
DASN51
DHIS54
DSER330
DGLY331
DALA334
DHOH544

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 D 500
ChainResidue
DSER1
DTYR360
DVAL361
DASN364
DHOH553
DHOH599

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 D 501
ChainResidue
DSER400
DASN401
DTHR402
DARG404
DSER405
DASP482

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE S62 A 499
ChainResidue
ATHR26
APRO29
AARG49
AASN51
ASER330
AGLY331
AHOH564

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 500
ChainResidue
ASER1
ATYR360
AVAL361
AASN364
AHOH557
AHOH566

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 501
ChainResidue
ASER400
AASN401
ATHR402
AARG404
ASER405

Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. ImIICKIENhQGV
ChainResidueDetails
DILE233-VAL245

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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