eF-site ID 4z9s-ABCD PDB Code 4z9s Chain A, B, C, D click to enlarge Title Non-covalent assembly of monoubiquitin that mimics K11 poly-ubiquitin Classification CELL CYCLE Compound Ubiquitin-40S ribosomal protein S27a Source Bos taurus (Bovine) (RS27A_BOVIN) Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG Description Functional site 1) chain A residue 37 type sequence P description binding site for residue MLA A 101 source : AC1 2) chain A residue 39 type sequence D description binding site for residue MLA A 101 source : AC1 3) chain A residue 40 type sequence Q description binding site for residue MLA A 101 source : AC1 4) chain A residue 74 type sequence R description binding site for residue MLA A 101 source : AC1 5) chain B residue 37 type sequence P description binding site for residue MLA A 101 source : AC1 6) chain B residue 39 type sequence D description binding site for residue MLA A 101 source : AC1 7) chain B residue 40 type sequence Q description binding site for residue MLA A 101 source : AC1 8) chain B residue 74 type sequence R description binding site for residue MLA A 101 source : AC1 9) chain A residue 15 type sequence L description binding site for residue MLA A 102 source : AC2 10) chain A residue 16 type sequence E description binding site for residue MLA A 102 source : AC2 11) chain A residue 32 type sequence D description binding site for residue MLA A 102 source : AC2 12) chain A residue 33 type sequence K description binding site for residue MLA A 102 source : AC2 13) chain B residue 24 type sequence E description binding site for residue MLA A 102 source : AC2 14) chain B residue 53 type sequence G description binding site for residue MLA A 102 source : AC2 15) chain A residue 49 type sequence Q description binding site for residue SCN A 103 source : AC3 16) chain A residue 52 type sequence D description binding site for residue SCN A 103 source : AC3 17) chain D residue 33 type sequence K description binding site for residue SCN A 103 source : AC3 18) chain A residue 6 type sequence K description binding site for residue SCN A 104 source : AC4 19) chain A residue 64 type sequence E description binding site for residue SCN A 104 source : AC4 20) chain B residue 4 type sequence F description binding site for residue SCN A 104 source : AC4 21) chain B residue 12 type sequence T description binding site for residue SCN A 104 source : AC4 22) chain A residue 7 type sequence T description binding site for residue SCN A 105 source : AC5 23) chain A residue 9 type sequence T description binding site for residue SCN A 105 source : AC5 24) chain A residue 48 type sequence K description binding site for residue SCN A 106 source : AC6 25) chain A residue 58 type sequence D description binding site for residue SCN A 106 source : AC6 26) chain A residue 59 type sequence Y description binding site for residue SCN A 106 source : AC6 27) chain D residue 54 type sequence R description binding site for residue SCN A 106 source : AC6 28) chain A residue 33 type sequence K description binding site for residue MLA B 101 source : AC7 29) chain B residue 42 type sequence R description binding site for residue MLA B 101 source : AC7 30) chain B residue 50 type sequence L description binding site for residue MLA B 101 source : AC7 31) chain B residue 51 type sequence E description binding site for residue MLA B 101 source : AC7 32) chain B residue 52 type sequence D description binding site for residue MLA B 101 source : AC7 33) chain B residue 72 type sequence R description binding site for residue MLA B 101 source : AC7 34) chain B residue 71 type sequence L description binding site for residue SCN B 102 source : AC8 35) chain B residue 33 type sequence K description binding site for residue SCN B 103 source : AC9 36) chain C residue 72 type sequence R description binding site for residue SCN B 103 source : AC9 37) chain B residue 14 type sequence T description binding site for residue MLA C 101 source : AD1 38) chain B residue 15 type sequence L description binding site for residue MLA C 101 source : AD1 39) chain B residue 16 type sequence E description binding site for residue MLA C 101 source : AD1 40) chain B residue 33 type sequence K description binding site for residue MLA C 101 source : AD1 41) chain C residue 51 type sequence E description binding site for residue MLA C 101 source : AD1 42) chain C residue 53 type sequence G description binding site for residue MLA C 101 source : AD1 43) chain C residue 54 type sequence R description binding site for residue MLA C 101 source : AD1 44) chain B residue 35 type sequence G description binding site for residue MLA C 102 source : AD2 45) chain C residue 35 type sequence G description binding site for residue MLA C 102 source : AD2 46) chain C residue 37 type sequence P description binding site for residue MLA C 102 source : AD2 47) chain C residue 39 type sequence D description binding site for residue MLA C 102 source : AD2 48) chain C residue 40 type sequence Q description binding site for residue MLA C 102 source : AD2 49) chain C residue 74 type sequence R description binding site for residue MLA C 102 source : AD2 50) chain D residue 37 type sequence P description binding site for residue MLA C 102 source : AD2 51) chain D residue 39 type sequence D description binding site for residue MLA C 102 source : AD2 52) chain D residue 40 type sequence Q description binding site for residue MLA C 102 source : AD2 53) chain D residue 74 type sequence R description binding site for residue MLA C 102 source : AD2 54) chain C residue 16 type sequence E description binding site for residue SCN C 103 source : AD3 55) chain D residue 53 type sequence G description binding site for residue SCN C 103 source : AD3 56) chain A residue 48 type sequence K description binding site for residue SCN C 104 source : AD4 57) chain A residue 49 type sequence Q description binding site for residue SCN C 104 source : AD4 58) chain A residue 51 type sequence E description binding site for residue SCN C 104 source : AD4 59) chain C residue 16 type sequence E description binding site for residue SCN C 104 source : AD4 60) chain C residue 33 type sequence K description binding site for residue MLA D 101 source : AD5 61) chain D residue 42 type sequence R description binding site for residue MLA D 101 source : AD5 62) chain D residue 50 type sequence L description binding site for residue MLA D 101 source : AD5 63) chain D residue 51 type sequence E description binding site for residue MLA D 101 source : AD5 64) chain D residue 52 type sequence D description binding site for residue MLA D 101 source : AD5 65) chain D residue 72 type sequence R description binding site for residue MLA D 101 source : AD5 66) chain B residue 35 type sequence G description binding site for residue SCN D 102 source : AD6 67) chain D residue 37 type sequence P description binding site for residue SCN D 102 source : AD6 68) chain D residue 40 type sequence Q description binding site for residue SCN D 102 source : AD6 69) chain A residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 70) chain A residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 71) chain B residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 72) chain B residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 73) chain C residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 74) chain C residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 75) chain D residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 76) chain D residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 77) chain A residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 78) chain B residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 79) chain C residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 80) chain D residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 81) chain A residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 82) chain B residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 83) chain B residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 84) chain B residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 85) chain B residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 86) chain B residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 87) chain C residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 88) chain C residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 89) chain C residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 90) chain C residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 91) chain C residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 92) chain A residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 93) chain C residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 94) chain C residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 95) chain D residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 96) chain D residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 97) chain D residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 98) chain D residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 99) chain D residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 100) chain D residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 101) chain D residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 102) chain A residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 103) chain A residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 104) chain A residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 105) chain A residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 106) chain A residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 107) chain B residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 108) chain B residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI5 109) chain A residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI3 110) chain B residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI3 111) chain C residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI3 112) chain D residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI3 113) chain A residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299

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