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5SCB

Structure of liver pyruvate kinase in complex with anthraquinone derivative 28

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 site: {"evidences":[{"source":"PubMed","id":"11960989","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VGB","evidenceCode":"ECO:0007744"}]}
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 Residues160
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11960989","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VGF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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