6CQF

Crystal structure of HPK1 in complex an inhibitor G1858

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue F97 A 301

Chain	Residue
A	LEU23
A	GLY97
A	ASP101
A	LEU144
A	HOH412
A	GLY24
A	VAL31
A	ALA44
A	MET91
A	GLU92
A	PHE93
A	CYS94
A	GLY95

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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	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ASP137

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU23
A	LYS46

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:24362026

Chain	Residue	Details
A	THR165
A	THR175

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:24362026

Chain	Residue	Details
A	ALA171

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