eF-site ID 5f95-AB PDB Code 5f95 Chain A, B click to enlarge Title Crystal structure of GSK3b in complex with Compound 18: 2-[(cyclopropylcarbonyl)amino]-N-(4-phenylpyridin-3-yl)pyridine-4-carboxamide Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Glycogen synthase kinase-3 beta Source Homo sapiens (Human) (GSK3B_HUMAN) Sequence A:  KVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKL CDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYF FYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPV IYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV LKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYT SSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGT PTREQIREMNPNFKFPQIKAHPWTKVFRPRTPPEAIALCS RLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPA LFNFTTQELSSNPPLATILIPPHAR B:  KVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKL CDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYF FYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPV IYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV LKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYT SSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGT PTREQIREMNPNPWTKVFRPRTPPEAIALCSRLLEYTPTA RLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQEL SSNPPLATILIPPHARIQ Description Functional site 1) chain A residue 85 type sequence K description binding site for residue 3UP A 401 source : AC1 2) chain A residue 132 type sequence L description binding site for residue 3UP A 401 source : AC1 3) chain A residue 133 type sequence D description binding site for residue 3UP A 401 source : AC1 4) chain A residue 134 type sequence Y description binding site for residue 3UP A 401 source : AC1 5) chain A residue 135 type sequence V description binding site for residue 3UP A 401 source : AC1 6) chain A residue 185 type sequence Q description binding site for residue 3UP A 401 source : AC1 7) chain A residue 188 type sequence L description binding site for residue 3UP A 401 source : AC1 8) chain A residue 200 type sequence D description binding site for residue 3UP A 401 source : AC1 9) chain B residue 83 type sequence A description binding site for residue 3UP B 401 source : AC2 10) chain B residue 85 type sequence K description binding site for residue 3UP B 401 source : AC2 11) chain B residue 132 type sequence L description binding site for residue 3UP B 401 source : AC2 12) chain B residue 133 type sequence D description binding site for residue 3UP B 401 source : AC2 13) chain B residue 134 type sequence Y description binding site for residue 3UP B 401 source : AC2 14) chain B residue 135 type sequence V description binding site for residue 3UP B 401 source : AC2 15) chain B residue 188 type sequence L description binding site for residue 3UP B 401 source : AC2 16) chain B residue 199 type sequence C description binding site for residue 3UP B 401 source : AC2 17) chain B residue 200 type sequence D description binding site for residue 3UP B 401 source : AC2 18) chain A residue 62-86 type prosite sequence IGNGSFGVVYQAKLCDSGELVAIKK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGNGSFGVVYqAklcdsgelv.........AIKK source prosite : PS00107 19) chain A residue 177-189 type prosite sequence ICHRDIKPQNLLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IcHrDIKpqNLLL source prosite : PS00108 20) chain A residue 181 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 21) chain B residue 181 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 22) chain A residue 62 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 62 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 85 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:17050006 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 85 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:17050006 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 216 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:25169422 source Swiss-Prot : SWS_FT_FI4 27) chain B residue 216 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:25169422 source Swiss-Prot : SWS_FT_FI4

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