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1OB3

Structure of P. falciparum PfPK5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006357biological_processregulation of transcription by RNA polymerase II
A0006468biological_processprotein phosphorylation
A0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0051726biological_processregulation of cell cycle
A0106310molecular_functionprotein serine kinase activity
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006357biological_processregulation of transcription by RNA polymerase II
B0006468biological_processprotein phosphorylation
B0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
B0046872molecular_functionmetal ion binding
B0051301biological_processcell division
B0051726biological_processregulation of cell cycle
B0106310molecular_functionprotein serine kinase activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkAqnnyget...........FALK
ChainResidueDetails
AILE10-LYS32

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI
ChainResidueDetails
AVAL121-ILE133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP125
BASP125

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE10
ALYS32
BILE10
BLYS32

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P24941
ChainResidueDetails
ATHR14
ATHR158
BTHR14
BTHR158

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P24941
ChainResidueDetails
ATYR15
BTYR15

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AGLN129
AASP125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BGLN129
BASP125

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS127
AASP125

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS127
BASP125

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS127
AASP125
ATHR163

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN130
ALYS127
AASP125

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN130
BLYS127
BASP125

222415

PDB entries from 2024-07-10

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