eF-site ID 1pin-A PDB Code 1pin Chain A click to enlarge Title PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS Classification ISOMERASE Compound PEPTIDYL-PROLYL CIS-TRANS ISOMERASE Source null (PIN1_HUMAN) Sequence A:  KLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGGKNGQG EPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELIN GYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQM QKPFEDASFALRTGEMSGPVFTDSGIHIILRTE Description Functional site 1) chain A residue 59 type sequence H description THE ACTIVE SITE OF THE PPIASE DOMAIN IS MARKED BY THE BOUND ALA-PRO DIPEPTIDE (CHAIN B). source : ACT 2) chain A residue 113 type sequence C description THE ACTIVE SITE OF THE PPIASE DOMAIN IS MARKED BY THE BOUND ALA-PRO DIPEPTIDE (CHAIN B). source : ACT 3) chain A residue 157 type sequence H description THE ACTIVE SITE OF THE PPIASE DOMAIN IS MARKED BY THE BOUND ALA-PRO DIPEPTIDE (CHAIN B). source : ACT 4) chain A residue 122 type sequence L description BINDING SITE FOR RESIDUE PRO A 202 source : AC2 5) chain A residue 129 type sequence Q description BINDING SITE FOR RESIDUE PRO A 202 source : AC2 6) chain A residue 130 type sequence M description BINDING SITE FOR RESIDUE PRO A 202 source : AC2 7) chain A residue 63 type sequence K description BINDING SITE FOR RESIDUE SO4 A 400 source : AC3 8) chain A residue 68 type sequence R description BINDING SITE FOR RESIDUE SO4 A 400 source : AC3 9) chain A residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 A 400 source : AC3 10) chain A residue 154 type sequence S description BINDING SITE FOR RESIDUE SO4 A 400 source : AC3 11) chain A residue 23 type sequence Y description BINDING SITE FOR RESIDUE 1PG A 300 source : AC4 12) chain A residue 32 type sequence S description BINDING SITE FOR RESIDUE 1PG A 300 source : AC4 13) chain A residue 33 type sequence Q description BINDING SITE FOR RESIDUE 1PG A 300 source : AC4 14) chain A residue 34 type sequence W description BINDING SITE FOR RESIDUE 1PG A 300 source : AC4 15) chain A residue 97 type sequence K description BINDING SITE FOR RESIDUE 1PG A 300 source : AC4 16) chain A residue 108 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17525332 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 46 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 71 type MOD_RES sequence S description Phosphoserine; by DAPK1 => ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:29686383 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 59 type catalytic sequence H description 511 source MCSA : MCSA1 20) chain A residue 113 type catalytic sequence C description 511 source MCSA : MCSA1 21) chain A residue 131 type catalytic sequence Q description 511 source MCSA : MCSA1 22) chain A residue 154 type catalytic sequence S description 511 source MCSA : MCSA1 23) chain A residue 157 type catalytic sequence H description 511 source MCSA : MCSA1 24) chain A residue 103-123 type prosite sequence FESLASQFSDCSSAKARGDLG description PPIC_PPIASE_1 PpiC-type peptidyl-prolyl cis-trans isomerase signature. FEsLAsqfSdcs.Saka..RGdLG source prosite : PS01096 25) chain A residue 11-37 type prosite sequence WEKRMSRSSGRVYYFNHITNASQWERP description WW_DOMAIN_1 WW/rsp5/WWP domain signature. WekrmsrssgrvYYfnhitnaSQWERP source prosite : PS01159

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