eF-site ID 2y5b-ABEF PDB Code 2y5b Chain A, B, E, F click to enlarge Title Structure of USP21 in complex with linear diubiquitin-aldehyde Classification PROTEIN BINDING/HYDROLASE Compound UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 21 Source Homo sapiens (Human) (UBB_HUMAN) Sequence A:  HTLLLGSGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLR RDFRQEVRAQELTEAFADVIGALWHPDSCEAVNPTRFRAV FQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRSDDDRA NLMWKRYLEREDSKIVDLFVGQLKSCLKCQACGYRSTTFE VFCDLSLPIPKKKVSLRDCFNLFTKEEELESENAPVCDRC RQKTRSTKKLTVQRFPRILVLHLNRFSASRGSIKKSSVGV DFPLQRLSLGDFASDSPVYQLYALCNHSGSVHYGHYTALC RCQTGWHVYNDSRVSPVSENQVASSEGYVLFYQLM B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLHMQIFVK TLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFA GKQLEDGRTLSDYNIQKESTLHLVLRLRGX E:  HHTLLLGSGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCL RRDFRQERAQELTEAFADVIGALWHPDSCEAVNPTRFRAV FQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGEEPEL SDDDRANLMWKRYLEREDSKIVDLFVGQLKSCLKCQACGY RSTTFEVFCDLSLPIPKGKVSLRDCFNLFTKEEELESENA PVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSASRGSIK KSSVGVDFPLQRLSLGDFASDKAGSPVYQLYALCNHSGSV HYGHYTALCRCQTGWHVYNDSRVSPVSENQVASSEGYVLF YQLMQ F:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGHMQIF VKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLI FAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX Description Functional site 1) chain A residue 384 type sequence C description BINDING SITE FOR RESIDUE ZN A 1000 source : AC1 2) chain A residue 387 type sequence C description BINDING SITE FOR RESIDUE ZN A 1000 source : AC1 3) chain A residue 437 type sequence C description BINDING SITE FOR RESIDUE ZN A 1000 source : AC1 4) chain A residue 440 type sequence C description BINDING SITE FOR RESIDUE ZN A 1000 source : AC1 5) chain A residue 472 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1559 source : AC2 6) chain A residue 473 type sequence I description BINDING SITE FOR RESIDUE SO4 A 1559 source : AC2 7) chain A residue 474 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1560 source : AC3 8) chain A residue 475 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1560 source : AC3 9) chain A residue 513 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1560 source : AC3 10) chain A residue 514 type sequence V description BINDING SITE FOR RESIDUE SO4 A 1560 source : AC3 11) chain F residue 54 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1560 source : AC3 12) chain E residue 235 type sequence P description BINDING SITE FOR RESIDUE SO4 E 1560 source : AC4 13) chain E residue 369 type sequence K description BINDING SITE FOR RESIDUE SO4 E 1560 source : AC4 14) chain E residue 457 type sequence R description BINDING SITE FOR RESIDUE SO4 E 1560 source : AC4 15) chain E residue 276 type sequence E description BINDING SITE FOR RESIDUE SO4 E 1561 source : AC5 16) chain E residue 277 type sequence A description BINDING SITE FOR RESIDUE SO4 E 1561 source : AC5 17) chain A residue 320 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1561 source : AC6 18) chain A residue 235 type sequence P description BINDING SITE FOR RESIDUE SO4 A 1562 source : AC7 19) chain A residue 369 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1562 source : AC7 20) chain A residue 457 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1562 source : AC7 21) chain A residue 483 type sequence P description BINDING SITE FOR RESIDUE SO4 A 1563 source : AC8 22) chain A residue 484 type sequence L description BINDING SITE FOR RESIDUE SO4 A 1563 source : AC8 23) chain A residue 485 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 1563 source : AC8 24) chain E residue 320 type sequence R description BINDING SITE FOR RESIDUE SO4 E 1562 source : AC9 25) chain A residue 541 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1564 source : BC1 26) chain A residue 543 type sequence N description BINDING SITE FOR RESIDUE SO4 A 1564 source : BC1 27) chain E residue 296 type sequence G description BINDING SITE FOR RESIDUE SO4 A 1564 source : BC1 28) chain A residue 515 type sequence H description BINDING SITE FOR RESIDUE SO4 B 1152 source : BC2 29) chain B residue 116 type sequence Q description BINDING SITE FOR RESIDUE SO4 B 1152 source : BC2 30) chain B residue 150 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1152 source : BC2 31) chain F residue 116 type sequence Q description BINDING SITE FOR RESIDUE SO4 F 1152 source : BC3 32) chain F residue 148 type sequence R description BINDING SITE FOR RESIDUE SO4 F 1152 source : BC3 33) chain F residue 150 type sequence R description BINDING SITE FOR RESIDUE SO4 F 1152 source : BC3 34) chain A residue 215 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1565 source : BC4 35) chain A residue 216 type sequence N description BINDING SITE FOR RESIDUE SO4 A 1565 source : BC4 36) chain A residue 390 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1565 source : BC4 37) chain A residue 534 type sequence D description BINDING SITE FOR RESIDUE SO4 A 1565 source : BC4 38) chain A residue 535 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1565 source : BC4 39) chain E residue 384 type sequence C description BINDING SITE FOR RESIDUE ZN E 1000 source : BC5 40) chain E residue 387 type sequence C description BINDING SITE FOR RESIDUE ZN E 1000 source : BC5 41) chain E residue 437 type sequence C description BINDING SITE FOR RESIDUE ZN E 1000 source : BC5 42) chain E residue 440 type sequence C description BINDING SITE FOR RESIDUE ZN E 1000 source : BC5 43) chain B residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 44) chain B residue 103-128 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 45) chain A residue 213-228 type prosite sequence GLRNLGNTCFLNAVLQ description USP_1 Ubiquitin specific protease (USP) domain signature 1. GLrnlGNtCFLNAvLQ source prosite : PS00972 46) chain A residue 502-519 type prosite sequence YQLYALCNHSGSVHYGHY description USP_2 Ubiquitin specific protease (USP) domain signature 2. YqLyALcnHsGsvhy..GHY source prosite : PS00973 47) chain B residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 48) chain B residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 49) chain F residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 50) chain F residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 51) 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 52) chain F 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 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 54) chain F 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 55) 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 56) chain F 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 57) chain B residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 58) chain F residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 59) 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 60) chain F 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 61) chain A residue 437 type MOD_RES sequence C 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 62) chain A residue 440 type MOD_RES sequence C 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 63) chain E residue 384 type MOD_RES sequence C 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 64) chain E residue 387 type MOD_RES sequence C 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 65) chain E residue 437 type MOD_RES sequence C 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 66) chain E residue 440 type MOD_RES sequence C 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 67) chain B residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 68) chain F residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 69) chain B residue 76 type MOD_RES sequence H description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 70) chain F residue 76 type MOD_RES sequence H description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 71) 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 72) chain F 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 73) chain B residue 76 type CROSSLNK sequence H description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 74) chain F residue 76 type CROSSLNK sequence H description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 75) 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 76) 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 77) chain F 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 78) chain F 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 79) 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 80) chain F 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

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