eF-site ID 4ksl-ABCDEFGHIJKLMNOPQRSTUVWX PDB Code 4ksl Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X Title Gumby/Fam105B in complex with linear di-ubiquitin Classification HYDROLASE Compound Protein FAM105B Source Homo sapiens (Human) (UBC_HUMAN) Sequence A:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLNEDLVDKIKESLTLLRKKWAGLAEM RTAEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYN DKEKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGG LEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPK DWPVVTLIAEDDRHYNIPVRVCE B:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLNEDLVDKIKESLTLLRKKWAGLAEM RTAEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYN DKEKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGG LEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPK DWPVVTLIAEDDRHYNIPVRVCE C:  GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQI FVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRL IFAGKQLEDGRTLSDYNIQKESTLHLVLRL D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIF VKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLI FAGKQLEDGRTLSDYNIQKESTLHLVLRL E:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLEDLVDKIKESLTLLRKKWAGLAEMR TAEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYND KEKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGL EQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKD WPVVTLIAEDDRHYNIPVRVCE F:  GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQI FVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRL IFAGKQLEDGRTLSDYNIQKESTLHLVLRL G:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLDLVDKIKESLTLLRKKWAGLAEMRT AEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYNDK EKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGLE QVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKDW PVVTLIAEDDRHYNIPVRVCE H:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIF VKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLI FAGKQLEDGRTLSDYNIQKESTLHLVLRL I:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLEDLVDKIKESLTLLRKKWAGLAEMR TAEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYND KEKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGL EQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKD WPVVTLIAEDDRHYNIPVRVCE J:  GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQI FVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRL IFAGKQLEDGRTLSDYNIQKESTLHLVLRL K:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLGLKFDGKNEDLVDKIKESLTLLRKK WAGLAEMRTAEARQIACDELFTNEAEEYSLYEAVKFLMLN RAIELYNDKEKGKEVPFFSVLLFARDTSNDPGQLLRNHLN QVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITV YPTDPPKDWPVVTLIAEDDRHYNIPVRVCE L:  GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQI FVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRL IFAGKQLEDGRTLSDYNIQKESTLHLVLRL M:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLGVDKIKESLTLLRKKWAGLAEMRTA EARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYNDKE KGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGLEQ VEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKDWP VVTLIAEDDRHYNIPVRVCE N:  GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQI FVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRL IFAGKQLEDGRTLSDYNIQKESTLHLVLRL O:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLGLKFDGKNEDLVDKIKESLTLLRKK WAGLAEMRTAEARQIACDELFTNEAEEYSLYEAVKFLMLN RAIELYNDKEKGKEVPFFSVLLFARDTSNDPGQLLRNHLN QVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITV YPTDPPKDWPVVTLIAEDDRHYNIPVRVCE P:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIF VKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLI FAGKQLEDGRTLSDYNIQKESTLHLVLRL Q:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLDLVDKIKESLTLLRKKWAGLAEMRT AEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYNDK EKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGLE QVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKDW PVVTLIAEDDRHYNIPVRVCE R:  GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQI FVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRL IFAGKQLEDGRTLSDYNIQKESTLHLVLRL S:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLGEDLVDKIKESLTLLRKKWAGLAEM RTAEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYN DKEKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGG LEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPK DWPVVTLIAEDDRHYNIPVRVCE T:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIF VKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLI FAGKQLEDGRTLSDYNIQKESTLHLVLRL U:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLDLVDKIKESLTLLRKKWAGLAEMRT AEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYNDK EKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGLE QVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKDW PVVTLIAEDDRHYNIPVRVCE V:  GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQI FVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRL IFAGKQLEDGRTLSDYNIQKESTLHLVLRL W:  RLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFT SIRRVRGDNYAALRATLFQAMSQAVGLPPWLQDPELMLLP EKLISKYNWIKQWKLLVDKIKESLTLLRKKWAGLAEMRTA EARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYNDKE KGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGLEQ VEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKDWP VVTLIAEDDRHYNIPVRVCE X:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIF VKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLI FAGKQLEDGRTLSDYNIQKESTLHLVLRL Description Functional site 1) chain S residue 129 type CROSSLNK sequence A description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 2) chain L residue 0 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 3) chain W residue 129 type CROSSLNK sequence A description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 4) chain N residue 0 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 5) chain R residue 0 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 6) chain B residue 129 type CROSSLNK sequence A description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 7) chain V residue 0 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 8) chain C residue 0 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 9) chain G residue 129 type CROSSLNK sequence A description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 10) chain F residue 0 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 11) chain K residue 129 type CROSSLNK sequence A description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 12) chain O residue 129 type CROSSLNK sequence A description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 13) chain J residue 0 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI2 14) chain V residue 0 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 15) chain M residue 126 type MOD_RES sequence D description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 16) chain M residue 339 type MOD_RES sequence H description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 17) chain O residue 126 type MOD_RES sequence D description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 18) chain O residue 339 type MOD_RES sequence H description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 19) chain Q residue 126 type MOD_RES sequence D description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 20) chain Q residue 339 type MOD_RES sequence H description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 21) chain S residue 126 type MOD_RES sequence D description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 22) chain C residue 0 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 23) chain S residue 339 type MOD_RES sequence H description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 24) chain U residue 126 type MOD_RES sequence D description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 25) chain U residue 339 type MOD_RES sequence H description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 26) chain W residue 126 type MOD_RES sequence D description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 27) chain W residue 339 type MOD_RES sequence H description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 28) chain F residue 0 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 29) chain J residue 0 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 30) chain L residue 0 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 31) chain N residue 0 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 32) chain R residue 0 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 34) chain S residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 35) chain U residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 36) chain W residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 37) chain B residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 38) chain E residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 39) chain G residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 40) chain I residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 41) chain K residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 42) chain M residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 43) chain O residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 44) chain Q residue 314 type SITE sequence E description Linear diubiquitin binding => ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0007744|PDB:3ZNZ, ECO:0007744|PDB:4KSK, ECO:0007744|PDB:4KSL source Swiss-Prot : SWS_FT_FI3 45) chain D residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 46) chain D residue 1027-1052 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299

Display surface Download Links