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1GNG

Glycogen synthase kinase-3 beta (GSK3) complex with FRATtide peptide

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 Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1385
ChainResidue
AARG96
AARG180
ALYS205
AASN213
AVAL214

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A1386
ChainResidue
AARG209
BARG209

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B1384
ChainResidue
BLYS205
BASN213
BVAL214
BARG96
BARG180

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1385
ChainResidue
AARG209
BVAL208
BARG209
BHOH2026

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE TRS B1386
ChainResidue
BARG96
BHOH2024

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

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WV60
ChainResidueDetails
ASER389
BSER389

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR390
BTHR390

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

222624

PDB entries from 2024-07-17

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