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3SD0

Identification of a Glycogen Synthase Kinase-3b Inhibitor that Attenuates Hyperactivity in CLOCK Mutant Mice

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 Residues13
DetailsBINDING SITE FOR RESIDUE TSK A 400
ChainResidue
AILE62
APRO136
ALEU188
ACYS199
AASP200
APHE67
AVAL70
AALA83
ALYS85
ALEU132
AASP133
ATYR134
AVAL135

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EPE A 401
ChainResidue
AHOH14
AARG96
AARG180
AGLY202
ALYS205
AASN213
AVAL214
AHOH459
AHOH466

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE TSK B 400
ChainResidue
BILE62
BGLY63
BPHE67
BVAL70
BLYS85
BVAL110
BLEU132
BASP133
BTYR134
BVAL135
BPRO136
BASN186
BLEU188
BCYS199
BASP200
BHOH460

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EPE B 401
ChainResidue
APHE291
ALYS292
BARG96
BARG180
BGLY202
BSER203
BALA204
BLYS205
BVAL214

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
ATYR216
BTYR216

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PDB entries from 2025-06-18

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