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3EOE

Crystal Structure of Pyruvate Kinase from toxoplasma gondii, 55.m00007

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004743molecular_functionpyruvate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0030955molecular_functionpotassium ion binding
A0032869biological_processcellular response to insulin stimulus
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004743molecular_functionpyruvate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0030955molecular_functionpotassium ion binding
B0032869biological_processcellular response to insulin stimulus
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004743molecular_functionpyruvate kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006096biological_processglycolytic process
C0016301molecular_functionkinase activity
C0030955molecular_functionpotassium ion binding
C0032869biological_processcellular response to insulin stimulus
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0004743molecular_functionpyruvate kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006096biological_processglycolytic process
D0016301molecular_functionkinase activity
D0030955molecular_functionpotassium ion binding
D0032869biological_processcellular response to insulin stimulus
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 512
ChainResidue
BTHR43
BARG66
BASN68
BSER347
BGLY348
BALA351
BHOH550

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 513
ChainResidue
BGLU257
BHOH672
BSER228
BLYS255

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL C 512
ChainResidue
CGLN122
CGLY123
CGLN180
CALA181

Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IrIIPKIENvEGL
ChainResidueDetails
AILE250-LEU262

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
ATHR313
ASER347
AGLU349
ALYS255
AARG66
AARG108

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
BTHR313
BSER347
BGLU349
BLYS255
BARG66
BARG108

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
CTHR313
CSER347
CGLU349
CLYS255
CARG66
CARG108

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
DTHR313
DSER347
DGLU349
DLYS255
DARG66

222036

PDB entries from 2024-07-03

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