eF-site ID 2ibi-AB PDB Code 2ibi Chain A, B click to enlarge Title Covalent Ubiquitin-USP2 Complex Classification HYDROLASE Compound Ubiquitin carboxyl-terminal hydrolase 2 Source Homo sapiens (Human) (UBIQ_HUMAN) Sequence A:  AQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMR DLHHGSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQ IQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRPKN PENLDHLPDDEKGRQMWRKYLEREDSRIGDLFVGQLKSSL TCTDCGYCSTVFDPFWDLSLPIAKRGPEVTLMDCMRLFTK EDVLDGDAAPTCCRCRGRKRCIKKFSIQRFPKILVLHLKR FSESRIRTSKLTTFVNFPLRDLDLREFASENTHAVYNLYA VSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQ VRTSDAYLLFYELAS B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG Description Functional site 1) chain A residue 425 type sequence C description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 2) chain A residue 428 type sequence C description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 3) chain A residue 476 type sequence C description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 4) chain A residue 479 type sequence C description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 5) chain A residue 274 type sequence N description BINDING SITE FOR RESIDUE NEH B 76 source : AC2 6) chain A residue 276 type sequence C description BINDING SITE FOR RESIDUE NEH B 76 source : AC2 7) chain A residue 355 type sequence Q description BINDING SITE FOR RESIDUE NEH B 76 source : AC2 8) chain A residue 556 type sequence G description BINDING SITE FOR RESIDUE NEH B 76 source : AC2 9) chain A residue 557 type sequence H description BINDING SITE FOR RESIDUE NEH B 76 source : AC2 10) chain B residue 75 type sequence G description BINDING SITE FOR RESIDUE NEH B 76 source : AC2 11) chain B residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 12) chain B residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 13) chain B residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 14) chain B residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 15) 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 16) chain B residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 17) chain A residue 268-283 type prosite sequence GLRNLGNTCFMNSILQ description USP_1 Ubiquitin specific protease (USP) domain signature 1. GLrnlGNtCFMNSiLQ source prosite : PS00972 18) chain A residue 541-558 type prosite sequence YNLYAVSNHSGTTMGGHY description USP_2 Ubiquitin specific protease (USP) domain signature 2. YnLyAVsnHsGttmg..GHY source prosite : PS00973 19) 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 20) 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 21) 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 22) 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 23) 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 24) chain A residue 429 type MOD_RES sequence G 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 A residue 477 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 26) chain A residue 480 type MOD_RES sequence R 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 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 28) 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

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