eF-site ID 4xkl-ABCD PDB Code 4xkl Chain A, B, C, D click to enlarge Title Crystal structure of NDP52 ZF2 in complex with mono-ubiquitin Classification PROTEIN BINDING/METAL BINDING PROTEIN Compound Ubiquitin Source Homo sapiens (Human) (CACO2_HUMAN) Sequence A:  GSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPP DQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG B:  PLCFNCPICDKIFPATEKQIFEDHVFCHSL C:  GSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPP DQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG D:  QPLCFNCPICDKIFPATEKQIFEDHVFCHSL Description Functional site 1) chain A residue 7 type sequence T description binding site for residue GOL A 101 source : AC1 2) chain A residue 8 type sequence L description binding site for residue GOL A 101 source : AC1 3) chain A residue 9 type sequence T description binding site for residue GOL A 101 source : AC1 4) chain A residue 69 type sequence L description binding site for residue GOL A 101 source : AC1 5) chain A residue 70 type sequence V description binding site for residue GOL A 101 source : AC1 6) chain A residue 71 type sequence L description binding site for residue GOL A 101 source : AC1 7) chain C residue 71 type sequence L description binding site for residue GOL A 101 source : AC1 8) chain B residue 426 type sequence D description binding site for residue ACT B 502 source : AC2 9) chain B residue 427 type sequence K description binding site for residue ACT B 502 source : AC2 10) chain B residue 428 type sequence I description binding site for residue ACT B 502 source : AC2 11) chain B residue 422 type sequence C description binding site for residue ZN B 503 source : AC3 12) chain B residue 425 type sequence C description binding site for residue ZN B 503 source : AC3 13) chain B residue 440 type sequence H description binding site for residue ZN B 503 source : AC3 14) chain B residue 444 type sequence H description binding site for residue ZN B 503 source : AC3 15) chain C residue 7 type sequence T description binding site for residue GOL C 101 source : AC4 16) chain C residue 8 type sequence L description binding site for residue GOL C 101 source : AC4 17) chain C residue 9 type sequence T description binding site for residue GOL C 101 source : AC4 18) chain C residue 69 type sequence L description binding site for residue GOL C 101 source : AC4 19) chain C residue 70 type sequence V description binding site for residue GOL C 101 source : AC4 20) chain C residue 71 type sequence L description binding site for residue GOL C 101 source : AC4 21) chain C residue 11 type sequence K description binding site for residue ACT C 102 source : AC5 22) chain C residue 12 type sequence T description binding site for residue ACT C 102 source : AC5 23) chain D residue 419 type sequence C description binding site for residue ACT D 501 source : AC6 24) chain D residue 422 type sequence C description binding site for residue ZN D 502 source : AC7 25) chain D residue 425 type sequence C description binding site for residue ZN D 502 source : AC7 26) chain D residue 440 type sequence H description binding site for residue ZN D 502 source : AC7 27) chain D residue 444 type sequence H description binding site for residue ZN D 502 source : AC7 28) chain B residue 422 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 425 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 440 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 444 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI2 32) chain D residue 422 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI2 33) chain D residue 425 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI2 34) chain D residue 440 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI2 35) chain D residue 444 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 419-444 type ZN_FING sequence CFNCPICDKIFPATEKQIFEDHVFCH description UBZ1-type => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI1 37) chain D residue 419-444 type ZN_FING sequence CFNCPICDKIFPATEKQIFEDHVFCH description UBZ1-type => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI1 38) chain C residue 54 type ZN_FING sequence R description UBZ1-type => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI1 39) chain C residue 72 type ZN_FING sequence R description UBZ1-type => ECO:0000255|PROSITE-ProRule:PRU01253 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 445 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 41) chain D residue 445 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 42) 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 43) 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 44) chain A residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 45) chain C residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 47) chain C residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 48) 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 49) 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 50) 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 51) 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 52) 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 53) 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 54) chain A residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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 62) chain A residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299

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