eF-site ID 2gse-ABCD PDB Code 2gse Chain A, B, C, D click to enlarge Title Crystal Structure of Human Dihydropyrimidinease-like 2 Classification HYDROLASE Compound Dihydropyrimidinase-related protein 2 Source Homo sapiens (Human) (DPYL2_HUMAN) Sequence A:  DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGG VKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTK AALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCD YSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRF QLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILD LGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITK VMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKN WAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHC TFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGK MDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDP DSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVL EDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLA B:  DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGG VKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTK AALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCD YSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRF QLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILD LGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITK VMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKN WAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHC TFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGK MDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDP DSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVL EDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLA C:  DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGG VKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTK AALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCD YSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRF QLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILD LGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITK VMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKN WAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHC TFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGK MDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDP DSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVL EDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLA D:  DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGG VKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTK AALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCD YSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRF QLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILD LGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITK VMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKN WAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHC TFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGK MDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDP DSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVL EDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLAE Description Functional site 1) chain A residue 81 type sequence Q description BINDING SITE FOR RESIDUE CA A 1000 source : AC1 2) chain A residue 349 type sequence T description BINDING SITE FOR RESIDUE CA A 1000 source : AC1 3) chain B residue 349 type sequence T description BINDING SITE FOR RESIDUE CA B 1001 source : AC2 4) chain C residue 349 type sequence T description BINDING SITE FOR RESIDUE CA C 1002 source : AC3 5) chain D residue 349 type sequence T description BINDING SITE FOR RESIDUE CA D 1003 source : AC4 6) chain A residue 32 type MOD_RES sequence Y description Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227 source Swiss-Prot : SWS_FT_FI1 7) chain B residue 32 type MOD_RES sequence Y description Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227 source Swiss-Prot : SWS_FT_FI1 8) chain C residue 32 type MOD_RES sequence Y description Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227 source Swiss-Prot : SWS_FT_FI1 9) chain D residue 32 type MOD_RES sequence Y description Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 258 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI2 11) chain B residue 258 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI2 12) chain C residue 258 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI2 13) chain D residue 258 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 259 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47942 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 259 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47942 source Swiss-Prot : SWS_FT_FI3 16) chain C residue 259 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47942 source Swiss-Prot : SWS_FT_FI3 17) chain D residue 259 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47942 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 431 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI4 19) chain B residue 431 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI4 20) chain C residue 431 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI4 21) chain D residue 431 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 465 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI5 23) chain B residue 465 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI5 24) chain C residue 465 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI5 25) chain D residue 465 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O08553 source Swiss-Prot : SWS_FT_FI5

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