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7M0L

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
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue YK4 A 301
ChainResidue
ALEU23
AGLY95
AGLY97
AASP101
ALEU144
ATYR28
AVAL31
AALA44
AVAL75
AMET91
AGLU92
APHE93
ACYS94

site_idAC2
Number of Residues13
Detailsbinding site for residue YK4 B 301
ChainResidue
BLEU23
BGLY24
BTYR28
BVAL31
BALA44
BVAL75
BMET91
BGLU92
BCYS94
BGLY95
BGLY97
BASP101
BLEU144

site_idAC3
Number of Residues13
Detailsbinding site for residue YK4 C 301
ChainResidue
CLEU23
CTYR28
CVAL31
CALA44
CVAL75
CMET91
CGLU92
CCYS94
CGLY95
CGLY97
CASP101
CLEU144
CPHE156

site_idAC4
Number of Residues13
Detailsbinding site for residue YK4 D 301
ChainResidue
DLEU23
DTYR28
DVAL31
DALA44
DVAL75
DMET91
DGLU92
DPHE93
DCYS94
DGLY95
DGLY97
DASP101
DLEU144

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 Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP137
BASP137
CASP137
DASP137

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
CLEU23
CLYS46
DLEU23
DLYS46
ALYS46
BLEU23
BLYS46
ALEU23

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:24362026
ChainResidueDetails
CGLU165
CTHR175
DGLU165
DTHR175
ATHR175
BGLU165
BTHR175
AGLU165

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:24362026
ChainResidueDetails
CGLU171
DGLU171
AGLU171
BGLU171

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PDB entries from 2024-06-12

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