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3SRK

A new class of suicide inhibitor blocks nucleotide binding to 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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LSA A 500
ChainResidue
AILE27
AGLY28
AASN51
AHIS54
ATYR59
AALA334
ALYS335

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K A 499
ChainResidue
AGLU240
AASP264

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A 501
ChainResidue
AGLN354
ALEU357
AGLU359

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PTK A 502
ChainResidue
AARG194
AARG194
ALYS224
ALYS224

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LSA B 500
ChainResidue
BILE27
BGLY28
BASN51
BHIS54
BTYR59
BALA334
BLYS335

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 499
ChainResidue
BGLN354
BLEU357
BGLU359
BHOH555

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K B 501
ChainResidue
BGLU240
BASP264

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 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

245011

PDB entries from 2025-11-19

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