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8FKO

Crystal structure of HPK1 kinase domain T165E,S171E phosphomimetic mutant in complex with 3-{4-[(2S,5R)-5-Amino-2-methylpiperidin-1-yl]-6-chloro-7H-pyrrolo[2,3-d]pyrimidin-5-yl}benzonitrile

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
E0004672molecular_functionprotein kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
F0004672molecular_functionprotein kinase activity
F0005524molecular_functionATP binding
F0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGTYGEVFkArdkvsgdl..........VALK
ChainResidueDetails
ALEU23-LYS46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP137
BASP137
CASP137
DASP137
EASP137
FASP137

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU23
ELYS46
FLEU23
FLYS46
ALYS46
BLEU23
BLYS46
CLEU23
CLYS46
DLEU23
DLYS46
ELEU23

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:24362026
ChainResidueDetails
AGLU165
ETHR175
FGLU165
FTHR175
ATHR175
BGLU165
BTHR175
CGLU165
CTHR175
DGLU165
DTHR175
EGLU165

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:24362026
ChainResidueDetails
AGLU171
BGLU171
CGLU171
DGLU171
EGLU171
FGLU171

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PDB entries from 2024-07-17

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