eF-site ID 4bos-ABCEF PDB Code 4bos Chain A, B, C, E, F click to enlarge Title Structure of OTUD2 OTU domain in complex with Ubiquitin K11-linked peptide Classification HYDROLASE Compound UBIQUITIN THIOESTERASE OTU1 Source (4BOS) Sequence A:  GPVLTRTVVPADNSALFTSVYYVVEGGVLNPACAPEMRRL IAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEI SILSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDG IHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELADEAR RRRQ B:  GPVLTRTVVPADNSALFTSVYYVVEGGVLNPACAPEMRRL IAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEI SILSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDG IHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELADEAR RRRQ C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG E:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR F:  TLTGKTI Description Functional site 1) chain A residue 212 type sequence W description BINDING SITE FOR RESIDUE NO3 B 1310 source : AC1 2) chain B residue 156 type sequence A description BINDING SITE FOR RESIDUE NO3 B 1310 source : AC1 3) chain B residue 157 type sequence D description BINDING SITE FOR RESIDUE NO3 B 1310 source : AC1 4) chain B residue 158 type sequence N description BINDING SITE FOR RESIDUE NO3 B 1310 source : AC1 5) chain B residue 159 type sequence S description BINDING SITE FOR RESIDUE NO3 B 1310 source : AC1 6) chain B residue 160 type sequence A description BINDING SITE FOR RESIDUE NO3 B 1310 source : AC1 7) chain B residue 267 type sequence H description BINDING SITE FOR RESIDUE NO3 B 1310 source : AC1 8) chain B residue 263 type sequence Y description BINDING SITE FOR RESIDUE NO3 B 1311 source : AC2 9) chain B residue 265 type sequence G description BINDING SITE FOR RESIDUE NO3 B 1311 source : AC2 10) chain B residue 251 type sequence E description BINDING SITE FOR RESIDUE MG B 1312 source : AC3 11) chain B residue 251 type sequence E description BINDING SITE FOR RESIDUE MG B 1312 source : AC3 12) chain B residue 251 type sequence E description BINDING SITE FOR RESIDUE MG B 1312 source : AC3 13) chain C residue 71 type sequence L description BINDING SITE FOR RESIDUE NO3 C 1077 source : AC4 14) chain A residue 222 type sequence A description BINDING SITE FOR RESIDUE NO3 C 1078 source : AC5 15) chain C residue 7 type sequence T description BINDING SITE FOR RESIDUE NO3 C 1078 source : AC5 16) chain C residue 8 type sequence L description BINDING SITE FOR RESIDUE NO3 C 1078 source : AC5 17) chain C residue 9 type sequence T description BINDING SITE FOR RESIDUE NO3 C 1078 source : AC5 18) chain C residue 69 type sequence L description BINDING SITE FOR RESIDUE NO3 C 1078 source : AC5 19) chain C residue 70 type sequence V description BINDING SITE FOR RESIDUE NO3 C 1078 source : AC5 20) chain C residue 71 type sequence L description BINDING SITE FOR RESIDUE NO3 C 1078 source : AC5 21) chain A residue 267 type sequence H description BINDING SITE FOR RESIDUE NO3 F 1014 source : AC6 22) chain A residue 306 type sequence R description BINDING SITE FOR RESIDUE NO3 F 1014 source : AC6 23) chain A residue 307 type sequence R description BINDING SITE FOR RESIDUE NO3 F 1014 source : AC6 24) chain F residue 9 type sequence T description BINDING SITE FOR RESIDUE NO3 F 1014 source : AC6 25) chain F residue 10 type sequence G description BINDING SITE FOR RESIDUE NO3 F 1014 source : AC6 26) chain F residue 11 type sequence K description BINDING SITE FOR RESIDUE NO3 F 1014 source : AC6 27) chain C residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 28) chain C residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 29) chain C residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 30) chain E residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 31) chain E residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 32) 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 33) chain E 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 34) 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 35) chain E 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 36) 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 37) chain E 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 38) chain C residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 39) chain E residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 40) 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 41) chain E 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 42) chain C residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 43) chain E residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 44) chain C residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 45) 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 46) chain E 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 47) chain C residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 48) 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 49) 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 50) chain E 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 51) chain E 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 52) 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 53) chain E 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

Display surface Download Links