eF-site ID 4k7u-ABC PDB Code 4k7u Chain A, B, C click to enlarge Title Crystal structure of Zn2.3-hUb (human ubiquitin) adduct from a solution 70 mM zinc acetate/1.3 mM hUb Classification LIGASE Compound ubiquitin Source Homo sapiens (Human) (UBC_HUMAN) Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR Description Functional site 1) chain A residue 1 type sequence M description BINDING SITE FOR RESIDUE ZN A 101 source : AC1 2) chain A residue 16 type sequence E description BINDING SITE FOR RESIDUE ZN A 101 source : AC1 3) chain B residue 51 type sequence E description BINDING SITE FOR RESIDUE ZN A 101 source : AC1 4) chain A residue 18 type sequence E description BINDING SITE FOR RESIDUE ZN A 102 source : AC2 5) chain C residue 21 type sequence D description BINDING SITE FOR RESIDUE ZN A 102 source : AC2 6) chain A residue 21 type sequence D description BINDING SITE FOR RESIDUE ZN A 103 source : AC3 7) chain B residue 18 type sequence E description BINDING SITE FOR RESIDUE ZN A 103 source : AC3 8) chain A residue 18 type sequence E description BINDING SITE FOR RESIDUE ZN A 104 source : AC4 9) chain B residue 18 type sequence E description BINDING SITE FOR RESIDUE ZN A 104 source : AC4 10) chain C residue 18 type sequence E description BINDING SITE FOR RESIDUE ZN A 104 source : AC4 11) chain A residue 14 type sequence T description BINDING SITE FOR RESIDUE ACT A 105 source : AC5 12) chain A residue 33 type sequence K description BINDING SITE FOR RESIDUE ACT A 105 source : AC5 13) chain A residue 16 type sequence E description BINDING SITE FOR RESIDUE EDO A 106 source : AC6 14) chain A residue 18 type sequence E description BINDING SITE FOR RESIDUE EDO A 106 source : AC6 15) chain A residue 21 type sequence D description BINDING SITE FOR RESIDUE EDO A 106 source : AC6 16) chain A residue 29 type sequence K description BINDING SITE FOR RESIDUE EDO A 106 source : AC6 17) chain B residue 18 type sequence E description BINDING SITE FOR RESIDUE EDO A 106 source : AC6 18) chain A residue 58 type sequence D description BINDING SITE FOR RESIDUE EDO A 107 source : AC7 19) chain B residue 15 type sequence L description BINDING SITE FOR RESIDUE EDO A 107 source : AC7 20) chain B residue 16 type sequence E description BINDING SITE FOR RESIDUE EDO A 107 source : AC7 21) chain B residue 29 type sequence K description BINDING SITE FOR RESIDUE EDO A 107 source : AC7 22) chain A residue 37 type sequence P description BINDING SITE FOR RESIDUE PEG A 108 source : AC8 23) chain A residue 39 type sequence D description BINDING SITE FOR RESIDUE PEG A 108 source : AC8 24) chain C residue 46 type sequence A description BINDING SITE FOR RESIDUE PEG A 108 source : AC8 25) chain C residue 68 type sequence H description BINDING SITE FOR RESIDUE PEG A 108 source : AC8 26) chain A residue 68 type sequence H description BINDING SITE FOR RESIDUE ZN B 101 source : AC9 27) chain B residue 6 type sequence K description BINDING SITE FOR RESIDUE ZN B 101 source : AC9 28) chain B residue 68 type sequence H description BINDING SITE FOR RESIDUE ZN B 101 source : AC9 29) chain B residue 1 type sequence M description BINDING SITE FOR RESIDUE ZN B 102 source : BC1 30) chain B residue 16 type sequence E description BINDING SITE FOR RESIDUE ZN B 102 source : BC1 31) chain C residue 51 type sequence E description BINDING SITE FOR RESIDUE ZN B 102 source : BC1 32) chain A residue 32 type sequence D description BINDING SITE FOR RESIDUE ZN B 103 source : BC2 33) chain C residue 51 type sequence E description BINDING SITE FOR RESIDUE ZN B 103 source : BC2 34) chain A residue 6 type sequence K description BINDING SITE FOR RESIDUE ACT B 104 source : BC3 35) chain A residue 66 type sequence T description BINDING SITE FOR RESIDUE ACT B 104 source : BC3 36) chain A residue 68 type sequence H description BINDING SITE FOR RESIDUE ACT B 104 source : BC3 37) chain B residue 6 type sequence K description BINDING SITE FOR RESIDUE ACT B 104 source : BC3 38) chain B residue 68 type sequence H description BINDING SITE FOR RESIDUE ACT B 104 source : BC3 39) chain A residue 63 type sequence K description BINDING SITE FOR RESIDUE EDO B 105 source : BC4 40) chain B residue 48 type sequence K description BINDING SITE FOR RESIDUE EDO B 105 source : BC4 41) chain B residue 49 type sequence Q description BINDING SITE FOR RESIDUE EDO B 105 source : BC4 42) chain C residue 31 type sequence Q description BINDING SITE FOR RESIDUE EDO B 105 source : BC4 43) chain C residue 32 type sequence D description BINDING SITE FOR RESIDUE EDO B 105 source : BC4 44) chain A residue 51 type sequence E description BINDING SITE FOR RESIDUE ZN C 101 source : BC5 45) chain C residue 1 type sequence M description BINDING SITE FOR RESIDUE ZN C 101 source : BC5 46) chain C residue 16 type sequence E description BINDING SITE FOR RESIDUE ZN C 101 source : BC5 47) chain B residue 21 type sequence D description BINDING SITE FOR RESIDUE ZN C 102 source : BC6 48) chain C residue 18 type sequence E description BINDING SITE FOR RESIDUE ZN C 102 source : BC6 49) chain B residue 16 type sequence E description BINDING SITE FOR RESIDUE ACT C 103 source : BC7 50) chain B residue 18 type sequence E description BINDING SITE FOR RESIDUE ACT C 103 source : BC7 51) chain B residue 21 type sequence D description BINDING SITE FOR RESIDUE ACT C 103 source : BC7 52) chain B residue 29 type sequence K description BINDING SITE FOR RESIDUE ACT C 103 source : BC7 53) chain C residue 18 type sequence E description BINDING SITE FOR RESIDUE ACT C 103 source : BC7 54) chain A residue 18 type sequence E description BINDING SITE FOR RESIDUE EDO C 104 source : BC8 55) chain C residue 18 type sequence E description BINDING SITE FOR RESIDUE EDO C 104 source : BC8 56) chain C residue 21 type sequence D description BINDING SITE FOR RESIDUE EDO C 104 source : BC8 57) chain C residue 29 type sequence K description BINDING SITE FOR RESIDUE EDO C 104 source : BC8 58) chain A residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 59) chain B residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 60) chain C residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 61) chain A residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 62) chain B residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 63) chain C residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 64) chain A residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 65) chain B residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 66) chain C residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 67) chain A residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 68) chain B residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 69) chain C residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 70) chain A residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 71) chain A residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 72) chain B residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 73) chain B residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 74) chain C residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 75) chain C residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 76) chain A residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 77) chain B residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 78) chain C residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 79) chain A residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 80) chain A residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 81) chain B residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 82) chain B residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 83) chain C residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 84) chain C residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 85) chain A residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 86) chain B residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 87) chain C residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 88) chain A residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 89) chain B residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 90) chain C residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 91) chain A residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 92) chain B residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 93) chain C residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 94) chain A residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299

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