eF-site ID 2xew-C PDB Code 2xew Chain C click to enlarge Title Crystal structure of K11-linked diubiquitin Classification CELL CYCLE Compound UBIQUITIN Source (UBIQ_HUMAN) Sequence C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR Description Functional site 1) chain C residue 15 type sequence L description BINDING SITE FOR RESIDUE EDO C 1075 source : AC8 2) chain C residue 16 type sequence E description BINDING SITE FOR RESIDUE EDO C 1075 source : AC8 3) chain C residue 29 type sequence K description BINDING SITE FOR RESIDUE EDO C 1075 source : AC8 4) chain C residue 33 type sequence K description BINDING SITE FOR RESIDUE EDO C 1075 source : AC8 5) chain C residue 2 type sequence Q description BINDING SITE FOR RESIDUE CL C 1076 source : AC9 6) chain C residue 63 type sequence K description BINDING SITE FOR RESIDUE CL C 1076 source : AC9 7) chain C residue 7 type sequence T description BINDING SITE FOR RESIDUE EDO E 1077 source : BC3 8) chain C residue 9 type sequence T description BINDING SITE FOR RESIDUE EDO E 1077 source : BC3 9) chain C residue 45 type sequence F description BINDING SITE FOR RESIDUE EDO I 1077 source : BC8 10) chain C residue 65 type sequence S description BINDING SITE FOR RESIDUE EDO I 1077 source : BC8 11) chain C residue 66 type sequence T description BINDING SITE FOR RESIDUE EDO I 1077 source : BC8 12) 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 13) chain C residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 14) chain C residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 15) chain C residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 16) chain C residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 17) 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 18) 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 19) 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 20) 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 21) 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 22) 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 23) 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

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