eF-site ID 3i3t-ABCDEFGH PDB Code 3i3t Chain A, B, C, D, E, F, G, H click to enlarge Title Crystal structure of covalent ubiquitin-USP21 complex Classification HYDROLASE Compound Ubiquitin carboxyl-terminal hydrolase 21 Source null (UBIQ_HUMAN) Sequence A:  HVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVQ ELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSG YSQQDAQEFLKLLMERLHLEINRRLSDDDRANLMWKRYLE REDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPI PKVSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTKKLT VQRFPRILVLHLNRFSASRGSIKKSSVGVDFPLQRLSLGD FASSPVYQLYALCNHSGSVHYGHYTALCRCQTGWHVYNDS RVSPVSENQVASSEGYVLFYQLM B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG C:  HVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVQ ELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSG YSQQDAQEFLKLLMERLHLEINRRLSDDDRANLMWKRYLE REDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPI PKKGFAGGKVSLRDCFNLFTKEEELESENAPVCDRCRQKT RSTKKLTVQRFPRILVLHLNRFSASRGSIKKSSVGVDFPL QRLSLGDFASSPVYQLYALCNHSGSVHYGHYTALCRCQTG WHVYNDSRVSPVSENQVASSEGYVLFYQLM D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG E:  HVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVQ ELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSG YSQQDAQEFLKLLMERLHLEINRRLSDDDRANLMWKRYLE REDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPI PKKGFAGGKVSLRDCFNLFTKEEELESENAPVCDRCRQKT RSTKKLTVQRFPRILVLHLNRFSASRGSIKKSSVGVDFPL QRLSLGDFASSPVYQLYALCNHSGSVHYGHYTALCRCQTG WHVYNDSRVSPVSENQVASSEGYVLFYQLM F:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG G:  HVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVQ ELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSG YSQQDAQEFLKLLMERLHLEINRRLSDDDRANLMWKRYLE REDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPI PKKVSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTKKL TVQRFPRILVLHLNRFSASRGSIKKSSVGVDFPLQRLSLG DFASSPVYQLYALCNHSGSVHYGHYTALCRCQTGWHVYND SRVSPVSENQVASSEGYVLFYQLM H:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG Description Functional site 1) chain A residue 384 type sequence C description BINDING SITE FOR RESIDUE ZN A 700 source : AC1 2) chain A residue 387 type sequence C description BINDING SITE FOR RESIDUE ZN A 700 source : AC1 3) chain A residue 437 type sequence C description BINDING SITE FOR RESIDUE ZN A 700 source : AC1 4) chain A residue 440 type sequence C description BINDING SITE FOR RESIDUE ZN A 700 source : AC1 5) chain C residue 384 type sequence C description BINDING SITE FOR RESIDUE ZN C 700 source : AC2 6) chain C residue 387 type sequence C description BINDING SITE FOR RESIDUE ZN C 700 source : AC2 7) chain C residue 437 type sequence C description BINDING SITE FOR RESIDUE ZN C 700 source : AC2 8) chain C residue 440 type sequence C description BINDING SITE FOR RESIDUE ZN C 700 source : AC2 9) chain E residue 384 type sequence C description BINDING SITE FOR RESIDUE ZN E 700 source : AC3 10) chain E residue 387 type sequence C description BINDING SITE FOR RESIDUE ZN E 700 source : AC3 11) chain E residue 437 type sequence C description BINDING SITE FOR RESIDUE ZN E 700 source : AC3 12) chain E residue 440 type sequence C description BINDING SITE FOR RESIDUE ZN E 700 source : AC3 13) chain G residue 384 type sequence C description BINDING SITE FOR RESIDUE ZN G 700 source : AC4 14) chain G residue 387 type sequence C description BINDING SITE FOR RESIDUE ZN G 700 source : AC4 15) chain G residue 437 type sequence C description BINDING SITE FOR RESIDUE ZN G 700 source : AC4 16) chain G residue 440 type sequence C description BINDING SITE FOR RESIDUE ZN G 700 source : AC4 17) chain A residue 219 type sequence N description BINDING SITE FOR RESIDUE NEH B 76 source : AC5 18) chain A residue 221 type sequence C description BINDING SITE FOR RESIDUE NEH B 76 source : AC5 19) chain A residue 517 type sequence G description BINDING SITE FOR RESIDUE NEH B 76 source : AC5 20) chain B residue 75 type sequence G description BINDING SITE FOR RESIDUE NEH B 76 source : AC5 21) chain C residue 219 type sequence N description BINDING SITE FOR RESIDUE NEH D 76 source : AC6 22) chain C residue 221 type sequence C description BINDING SITE FOR RESIDUE NEH D 76 source : AC6 23) chain C residue 299 type sequence Q description BINDING SITE FOR RESIDUE NEH D 76 source : AC6 24) chain C residue 517 type sequence G description BINDING SITE FOR RESIDUE NEH D 76 source : AC6 25) chain C residue 518 type sequence H description BINDING SITE FOR RESIDUE NEH D 76 source : AC6 26) chain D residue 75 type sequence G description BINDING SITE FOR RESIDUE NEH D 76 source : AC6 27) chain E residue 219 type sequence N description BINDING SITE FOR RESIDUE NEH F 76 source : AC7 28) chain E residue 221 type sequence C description BINDING SITE FOR RESIDUE NEH F 76 source : AC7 29) chain E residue 299 type sequence Q description BINDING SITE FOR RESIDUE NEH F 76 source : AC7 30) chain E residue 517 type sequence G description BINDING SITE FOR RESIDUE NEH F 76 source : AC7 31) chain F residue 75 type sequence G description BINDING SITE FOR RESIDUE NEH F 76 source : AC7 32) chain G residue 219 type sequence N description BINDING SITE FOR RESIDUE NEH H 76 source : AC8 33) chain G residue 221 type sequence C description BINDING SITE FOR RESIDUE NEH H 76 source : AC8 34) chain G residue 299 type sequence Q description BINDING SITE FOR RESIDUE NEH H 76 source : AC8 35) chain G residue 517 type sequence G description BINDING SITE FOR RESIDUE NEH H 76 source : AC8 36) chain H residue 75 type sequence G description BINDING SITE FOR RESIDUE NEH H 76 source : AC8 37) 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_FI10 38) chain D 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_FI10 39) 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_FI10 40) chain H 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_FI10 41) chain B residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 42) chain D residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 43) chain F residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 44) chain H residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 45) 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_FI5 46) 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_FI5 47) chain D 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_FI5 48) chain H 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_FI5 49) 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_FI6 50) chain D 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_FI6 51) 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_FI6 52) chain H 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_FI6 53) 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_FI7 54) 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_FI7 55) 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_FI7 56) chain H 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_FI7 57) chain H 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_FI7 58) 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_FI7 59) chain D 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_FI7 60) chain D 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_FI7 61) chain F residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 62) chain F residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 63) chain H residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 64) chain H residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 65) chain B residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 66) chain B residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 67) chain D residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 68) chain D residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 69) chain B residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 70) chain D residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 71) chain F residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 72) chain H residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 73) 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 74) chain D 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 75) 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 76) chain H 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 77) chain C 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 78) chain C 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 79) chain C 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 80) chain C 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 81) 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 82) 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 83) 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 84) 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 85) chain G 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 86) chain G 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 87) chain G 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 88) chain G 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:25474007, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 89) chain B residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 90) chain A residue 213-228 type prosite sequence GLRNLGNTCFLNAVLQ description USP_1 Ubiquitin specific protease (USP) domain signature 1. GLrnlGNtCFLNAvLQ source prosite : PS00972 91) chain A residue 502-519 type prosite sequence YQLYALCNHSGSVHYGHY description USP_2 Ubiquitin specific protease (USP) domain signature 2. YqLyALcnHsGsvhy..GHY source prosite : PS00973 92) 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_FI9 93) chain D 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_FI9 94) 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_FI9 95) chain H 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_FI9 96) 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_FI8 97) chain D 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_FI8 98) 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_FI8 99) chain H 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_FI8

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