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7L24

HPK1 IN COMPLEX WITH COMPOUND 11

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 Residues11
Detailsbinding site for residue XHV A 301
ChainResidue
AVAL31
ALEU144
AASP155
AALA44
AMET91
AGLU92
ACYS94
AGLY95
AGLY97
AASP101
AALA141

site_idAC2
Number of Residues13
Detailsbinding site for residue XHV B 301
ChainResidue
BLEU23
BVAL31
BALA44
BLYS46
BMET91
BGLU92
BCYS94
BGLY95
BGLY97
BASP101
BALA141
BASN142
BLEU144

site_idAC3
Number of Residues12
Detailsbinding site for residue XHV C 301
ChainResidue
CALA44
CLYS46
CMET91
CGLU92
CPHE93
CCYS94
CGLY95
CGLY97
CALA141
CLEU144
CASP155
DASP217

site_idAC4
Number of Residues12
Detailsbinding site for residue XHV D 301
ChainResidue
DLEU23
DVAL31
DALA44
DMET91
DGLU92
DCYS94
DGLY95
DALA96
DGLY97
DALA141
DLEU144
DASP155

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
ALEU23
ALYS46
BLEU23
BLYS46
CLEU23
CLYS46
DLEU23
DLYS46

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:24362026
ChainResidueDetails
ATHR165
ATHR175
BTHR165
BTHR175
CTHR165
CTHR175
DTHR165
DTHR175

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:24362026
ChainResidueDetails
AALA171
BALA171
CALA171
DALA171

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PDB entries from 2024-07-17

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