eF-site ID 3mtn-ABCD PDB Code 3mtn Chain A, B, C, D click to enlarge Title Usp21 in complex with a ubiquitin-based, USP21-specific inhibitor Classification HYDROLASE Compound Ubiquitin carboxyl-terminal hydrolase 21 Source Homo sapiens (Human) (P62988) Sequence A:  GHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEV PGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQK YVPSFSGYSQQDAQEFLKLLMERLHLEINRRLSDDDRANL MWKRYLEREDSKIVDLFVGQLKSCLKCQACGYRSTTFEVF CDLSLPIPKKGFAGGKVSLRDCFNLFTKEEELESENAPVC DRCRQKTRSTKKLTVQRFPRILVLHLNRFSARGSIKKSSV GVDFPLQRLSLGDFASSPVYQLYALCNHSGSVHYGHYTAL CRCQTGWHVYNDSRVSPVSENQVASSEGYVLFYQLM B:  HMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKWSTLFLLLRLRGG C:  GHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEV PGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQK YVPSFSGYSQQDAQEFLKLLMERLHLEINRRSDDDRANLM WKRYLEREDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFC DLSLPIPKKGFGKVSLRDCFNLFTKEEELESENAPVCDRC RQKTRSTKKLTVQRFPRILVLHLNRFSASRGSIKKSSVGV DFPLQRLSLGDFASSPVYQLYALCNHSGSVHYGHYTALCR CQTGWHVYNDSRVSPVSENQVASSEGYVLFYQLM D:  HMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKWSTLFLLLRLRGG 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 A residue 401 type sequence S description BINDING SITE FOR RESIDUE CL A 1 source : AC3 10) chain B residue 68 type sequence F description BINDING SITE FOR RESIDUE CL A 1 source : AC3 11) chain C residue 401 type sequence S description BINDING SITE FOR RESIDUE CL C 1 source : AC4 12) chain D residue 68 type sequence F description BINDING SITE FOR RESIDUE CL C 1 source : AC4 13) chain A residue 360 type sequence K description BINDING SITE FOR RESIDUE CL A 563 source : AC5 14) chain A residue 454 type sequence R description BINDING SITE FOR RESIDUE CL A 563 source : AC5 15) chain A residue 311 type sequence E description BINDING SITE FOR RESIDUE GOL A 2 source : AC6 16) chain A residue 314 type sequence H description BINDING SITE FOR RESIDUE GOL A 2 source : AC6 17) chain A residue 370 type sequence I description BINDING SITE FOR RESIDUE GOL A 2 source : AC6 18) chain C residue 311 type sequence E description BINDING SITE FOR RESIDUE GOL C 3 source : AC7 19) chain C residue 314 type sequence H description BINDING SITE FOR RESIDUE GOL C 3 source : AC7 20) chain C residue 370 type sequence I description BINDING SITE FOR RESIDUE GOL C 3 source : AC7 21) chain C residue 371 type sequence V description BINDING SITE FOR RESIDUE GOL C 3 source : AC7 22) chain D residue 47 type sequence G description BINDING SITE FOR RESIDUE GOL C 3 source : AC7 23) chain A residue 417 type sequence R description BINDING SITE FOR RESIDUE CL A 564 source : AC8 24) 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 25) 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:25527291 source Swiss-Prot : SWS_FT_FI3 26) 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 27) 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 28) 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:25527291 source Swiss-Prot : SWS_FT_FI3 29) 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:25527291 source Swiss-Prot : SWS_FT_FI3 30) 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:25527291 source Swiss-Prot : SWS_FT_FI3 31) 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:25527291 source Swiss-Prot : SWS_FT_FI3 32) 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 33) 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_FI12 34) chain B residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 35) chain D residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 37) chain D residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 38) 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 39) 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_FI6 40) chain B residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 41) chain D residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 42) 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 43) 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 44) 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_FI8 45) 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_FI8 46) chain B residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 47) chain B residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 48) chain D residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 49) chain D residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 50) chain B residue 68 type SITE sequence F description Essential for function source Swiss-Prot : SWS_FT_FI2 51) chain D residue 68 type SITE sequence F description Essential for function source Swiss-Prot : SWS_FT_FI2 52) 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 53) 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_FI10 54) 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 55) 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_FI11 56) 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 57) 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_FI9 58) chain A residue 213-228 type prosite sequence GLRNLGNTCFLNAVLQ description USP_1 Ubiquitin specific protease (USP) domain signature 1. GLrnlGNtCFLNAvLQ source prosite : PS00972 59) chain A residue 502-519 type prosite sequence YQLYALCNHSGSVHYGHY description USP_2 Ubiquitin specific protease (USP) domain signature 2. YqLyALcnHsGsvhy..GHY source prosite : PS00973 60) chain B residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299

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