8FH4

Crystal structure of HPK1 kinase domain T165E,S171E phosphomimetic mutant in complex with 3-[6-chloro-4-(9-methyl-1-oxa-4,9-diazaspiro[5.5]undec-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-5-yl]benzonitrile

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGTYGEVFkArdkvsgdl..........VALK

Chain	Residue	Details
A	LEU23-LYS46

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ASP137
B	ASP137
C	ASP137
D	ASP137

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU23
A	LYS46
B	LEU23
B	LYS46
C	LEU23
C	LYS46
D	LEU23
D	LYS46

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site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:24362026

Chain	Residue	Details
A	GLU165
A	THR175
B	GLU165
B	THR175
C	GLU165
C	THR175
D	GLU165
D	THR175

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:24362026

Chain	Residue	Details
A	GLU171
B	GLU171
C	GLU171
D	GLU171

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