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3F88

glycogen synthase Kinase 3beta inhibitor complex

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 Residues12
DetailsBINDING SITE FOR RESIDUE 3HT A 999
ChainResidue
AILE62
AASP200
A2HT998
AHOH1100
APHE67
AVAL70
AALA83
ALYS85
AASP133
ATYR134
AVAL135
ACYS199

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 2HT A 998
ChainResidue
AGLY63
APHE67
AVAL70
AGLN185
AASN186
AASP200
A3HT999

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 3HT B 999
ChainResidue
BILE62
BPHE67
BVAL70
BALA83
BLYS85
BLEU132
BASP133
BTYR134
BVAL135
BPRO136
BTHR138
BARG141
BLEU188
BCYS199
BASP200
B2HT998

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 2HT B 998
ChainResidue
BGLY63
BPHE67
BVAL70
BGLN185
BASN186
BASP200
B3HT999
BHOH1113

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
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17050006","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"12554650","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25169422","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP181
AGLN185

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP181
BGLN185

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP181
ALYS183

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP181
BLYS183

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP181
ALYS183
ASER219

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP181
BLYS183
BSER219

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP181
AASN186
ALYS183

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP181
BASN186
BLYS183

239803

PDB entries from 2025-08-06

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