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

3GG8

Crystal structure of the Toxoplasma gondii Pyruvate Kinase N terminal truncated

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
ATHR437
AGLU438
ATHR439
AGLY440
ATHR442
AGLY513

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 532
ChainResidue
AHOH564
AARG86
AASN88
ASER367

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 532
ChainResidue
BTHR437
BGLU438
BTHR439
BGLY440
BGLN441
BTHR442
BHOH594

Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IrIIPKIENvEGL
ChainResidueDetails
AILE270-LEU282

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
AARG86
AGLU369
ALYS275
ATHR333
ASER367
AARG128

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
BARG86
BGLU369
BLYS275
BTHR333
BSER367
BARG128

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
CARG86
CGLU369
CLYS275
CTHR333
CSER367
CARG128

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
DARG86
DGLU369
DLYS275
DTHR333
DSER367
DARG128

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon