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3HQP

Crystal structure of Leishmania mexicana pyruvate kinase (LmPYK) in complex with ATP, Oxalate and fructose 2,6 bisphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004743molecular_functionpyruvate kinase activity
A0006096biological_processglycolytic process
A0006950biological_processresponse to stress
A0030955molecular_functionpotassium ion binding
B0000287molecular_functionmagnesium ion binding
B0004743molecular_functionpyruvate kinase activity
B0006096biological_processglycolytic process
B0006950biological_processresponse to stress
B0030955molecular_functionpotassium ion binding
C0000287molecular_functionmagnesium ion binding
C0004743molecular_functionpyruvate kinase activity
C0006096biological_processglycolytic process
C0006950biological_processresponse to stress
C0030955molecular_functionpotassium ion binding
D0000287molecular_functionmagnesium ion binding
D0004743molecular_functionpyruvate kinase activity
D0006096biological_processglycolytic process
D0006950biological_processresponse to stress
D0030955molecular_functionpotassium ion binding
E0000287molecular_functionmagnesium ion binding
E0004743molecular_functionpyruvate kinase activity
E0006096biological_processglycolytic process
E0006950biological_processresponse to stress
E0030955molecular_functionpotassium ion binding
F0000287molecular_functionmagnesium ion binding
F0004743molecular_functionpyruvate kinase activity
F0006096biological_processglycolytic process
F0006950biological_processresponse to stress
F0030955molecular_functionpotassium ion binding
G0000287molecular_functionmagnesium ion binding
G0004743molecular_functionpyruvate kinase activity
G0006096biological_processglycolytic process
G0006950biological_processresponse to stress
G0030955molecular_functionpotassium ion binding
H0000287molecular_functionmagnesium ion binding
H0004743molecular_functionpyruvate kinase activity
H0006096biological_processglycolytic process
H0006950biological_processresponse to stress
H0030955molecular_functionpotassium ion binding
I0000287molecular_functionmagnesium ion binding
I0004743molecular_functionpyruvate kinase activity
I0006096biological_processglycolytic process
I0006950biological_processresponse to stress
I0030955molecular_functionpotassium ion binding
J0000287molecular_functionmagnesium ion binding
J0004743molecular_functionpyruvate kinase activity
J0006096biological_processglycolytic process
J0006950biological_processresponse to stress
J0030955molecular_functionpotassium ion binding
K0000287molecular_functionmagnesium ion binding
K0004743molecular_functionpyruvate kinase activity
K0006096biological_processglycolytic process
K0006950biological_processresponse to stress
K0030955molecular_functionpotassium ion binding
L0000287molecular_functionmagnesium ion binding
L0004743molecular_functionpyruvate kinase activity
L0006096biological_processglycolytic process
L0006950biological_processresponse to stress
L0030955molecular_functionpotassium ion binding
M0000287molecular_functionmagnesium ion binding
M0004743molecular_functionpyruvate kinase activity
M0006096biological_processglycolytic process
M0006950biological_processresponse to stress
M0030955molecular_functionpotassium ion binding
N0000287molecular_functionmagnesium ion binding
N0004743molecular_functionpyruvate kinase activity
N0006096biological_processglycolytic process
N0006950biological_processresponse to stress
N0030955molecular_functionpotassium ion binding
O0000287molecular_functionmagnesium ion binding
O0004743molecular_functionpyruvate kinase activity
O0006096biological_processglycolytic process
O0006950biological_processresponse to stress
O0030955molecular_functionpotassium ion binding
P0000287molecular_functionmagnesium ion binding
P0004743molecular_functionpyruvate kinase activity
P0006096biological_processglycolytic process
P0006950biological_processresponse to stress
P0030955molecular_functionpotassium ion binding
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 Residues144
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues64
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

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PDB entries from 2026-05-27

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