eF-site ID 1cmx-ABCD PDB Code 1cmx Chain A, B, C, D click to enlarge Title STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES Classification HYDROLASE Compound PROTEIN (UBIQUITIN YUH1-UBAL) Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (UBIQ_HUMANX) Sequence A:  RAVVPIESNPEVFTNFAHKLGLKNEWAYFDIYSLTEPELL AFLPRPVKAIVLLFPINDVIWFKQSVKNACGLYAILHSLS NNQSLLEPGSDLDNFLKSQSDTSSSKNRFDDVTTDQFVLN VIKENVQTFSTGQSEAPEATADTNLHYITYVEENGGIFEL DGRNLSGPLYLGKSDPTATDLIEQELVRVRVASYMENANE EDVLNFAMLGLGPN B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX C:  AVVPIESNPEVFTNFAHKLGLKNEWAYFDIYSLTEPELLA FLPRPVKAIVLLFPVIWFKQSVKNACGLYAILHSLSNNQS LLEPGSDLDNFLKSQSDTSSSKNRFDDVTTDQFVLNVIKE NVQTFSTGQSEAPEATADTNLHYITYVEENGGIFELDGRN LSGPLYLGKSDPTATDLIEQELVRVRVASYMENANEEDVL NFAMLGLGPN D:  KTLTGQQRLLVLRLRGX Description Functional site 1) chain A residue 90 type sequence C description CYSTEINE PROTEASE source : CAT 2) chain A residue 166 type sequence H description CYSTEINE PROTEASE source : CAT 3) chain A residue 181 type sequence D description CYSTEINE PROTEASE source : CAT 4) chain C residue 490 type sequence C description CYSTEINE PROTEASE source : CAT 5) chain C residue 566 type sequence H description CYSTEINE PROTEASE source : CAT 6) chain C residue 581 type sequence D description CYSTEINE PROTEASE source : CAT 7) chain B residue 354 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 8) chain B residue 372 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 9) chain D residue 772 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 10) chain B residue 368 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 11) chain B residue 366 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI10 12) chain A residue 181 type CROSSLNK sequence D 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_FI4 13) chain B residue 363 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_FI4 14) chain B residue 365 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_FI9 15) chain B residue 306 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_FI3 16) chain D residue 706 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_FI3 17) chain B residue 333 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_FI8 18) chain B residue 311 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_FI5 19) chain B residue 348 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_FI5 20) chain B residue 327 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_FI6 21) chain B residue 329 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_FI7 22) chain B residue 327-352 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 23) chain A residue 84-100 type prosite sequence QSVKNACGLYAILHSLS description UCH_1 Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site. QsvkNACGlyaILHSLS source prosite : PS00140

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