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6HK4

Crystal structure of GSK-3B in complex with pyrazine inhibitor C22

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 Residues6
Detailsbinding site for residue MLI A 401
ChainResidue
AARG96
AARG180
ALYS205
AASN213
AVAL214
AHOH520

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 402
ChainResidue
ALYS86
AASN129
ATYR56
ATHR59
ATYR71

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 403
ChainResidue
APTR216
AARG220
ATYR221

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 404
ChainResidue
AARG220
BLYS183
BGLN185
BSER219

site_idAC5
Number of Residues3
Detailsbinding site for residue DMS A 405
ChainResidue
ATYR146
ATYR157
ATYR161

site_idAC6
Number of Residues5
Detailsbinding site for residue DMS A 406
ChainResidue
ATHR138
AGLN185
AASN186
ADMS407
AG8E408

site_idAC7
Number of Residues7
Detailsbinding site for residue DMS A 407
ChainResidue
ATHR138
ATYR140
AARG141
AGLN185
ADMS406
AG8E408
BASP260

site_idAC8
Number of Residues14
Detailsbinding site for residue G8E A 408
ChainResidue
AILE62
APHE67
ALYS85
AVAL110
AASP133
ATYR134
AVAL135
APRO136
AARG141
ALEU188
AASP200
ADMS406
ADMS407
AHOH530

site_idAC9
Number of Residues7
Detailsbinding site for residue MLI B 401
ChainResidue
BARG96
BARG180
BLYS205
BGLU211
BVAL214
BHOH506
BHOH554

site_idAD1
Number of Residues4
Detailsbinding site for residue GOL B 402
ChainResidue
BTYR56
BTYR71
BLYS86
BASN129

site_idAD2
Number of Residues6
Detailsbinding site for residue GOL B 403
ChainResidue
BTYR140
BALA143
BARG144
BSER147
BGLU249
BGLY253

site_idAD3
Number of Residues5
Detailsbinding site for residue GOL B 404
ChainResidue
ATYR140
AGLN185
BARG220
BTYR221
BASP260

site_idAD4
Number of Residues4
Detailsbinding site for residue GOL B 405
ChainResidue
BASP181
BSER203
BCYS218
BSER219

site_idAD5
Number of Residues4
Detailsbinding site for residue DMS B 406
ChainResidue
APRO51
BTYR146
BTYR157
BTYR161

site_idAD6
Number of Residues6
Detailsbinding site for residue DMS B 407
ChainResidue
AASP260
BTHR138
BTYR140
BARG141
BGLN185
BG8E409

site_idAD7
Number of Residues4
Detailsbinding site for residue DMS B 408
ChainResidue
BTHR138
BGLN185
BASN186
BG8E409

site_idAD8
Number of Residues17
Detailsbinding site for residue G8E B 409
ChainResidue
BARG141
BLEU188
BASP200
BDMS407
BDMS408
AHOH533
BLYS60
BILE62
BPHE67
BVAL70
BALA83
BLYS85
BLEU132
BASP133
BTYR134
BVAL135
BPRO136

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGNGSFGVVYqAklcdsgelv.........AIKK
ChainResidueDetails
AILE62-LYS86

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IcHrDIKpqNLLL
ChainResidueDetails
AILE177-LEU189

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP181
BASP181

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE62
BILE62

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:17050006
ChainResidueDetails
ALYS85
BLYS85

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:25169422
ChainResidueDetails
APTR216
BPTR216

219869

PDB entries from 2024-05-15

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