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7M0M

HPK1 IN COMPLEX WITH COMPOUND 1

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
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue YK1 A 301
ChainResidue
ALEU23
AASP101
AASN142
ALEU144
AALA154
AASP155
AHOH449
AGLY25
AVAL31
AMET91
AGLU92
APHE93
ACYS94
AGLY95
AGLY97

site_idAC2
Number of Residues16
Detailsbinding site for residue YK1 B 301
ChainResidue
BLEU23
BGLY25
BVAL31
BVAL75
BMET91
BGLU92
BPHE93
BCYS94
BGLY95
BGLY97
BASP101
BASN142
BLEU144
BALA154
BASP155
BHOH447

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP137
BASP137

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU23
ALYS46
BLEU23
BLYS46

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:24362026
ChainResidueDetails
AGLU165
ATHR175
BGLU165
BTHR175

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:24362026
ChainResidueDetails
AGLU171
BGLU171

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PDB entries from 2024-11-13

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