eF-site ID 1nbf-ABCDE PDB Code 1nbf Chain A, B, C, D, E click to enlarge Title Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde Classification HYDROLASE Compound Ubiquitin carboxyl-terminal hydrolase 7 Source (UBIQ_HUMAN) Sequence A:  KKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPT EGDDSSKSVPLALQRVFYELQHSDKPVGTKKLTKSFGWET LDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGK MVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFVDY VAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLM RFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKTDPKDPAN YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSR CTKEEAIEHNYGGHDDDLSVRHCTNAYMLVYIRESKLSEV LQAVTDHDIPQQLVERLQEEKRIEAQK B:  KKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPT EGDDSSKSVPLALQRVFYELQHSDKPVGTKKLTKSFGWET LDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGK MVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFVDY VAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLM RFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKTDPKDPAN YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSR CTKEEAIEHNYGGHDDDLSVRHCTNAYMLVYIRESKLSEV LQAVTDHDIPQQLVERLQEEKRIEAQK C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX E:  KKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPT EGDDSSKSVPLALQRVFYELQHSDKPVGTKKLTKSFGWET LDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGK MVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFVDY VAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLM RFMNIKINDRFEFPEQLPLDEFLQKTDPKDPANYILHAVL VHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAI EHNYGGHDDDLSVRHCTNAYMLVYIRESKLSEVLQAVTDH DIPQQLVERLQEEKRIEAQK Description (1)  Ubiquitin carboxyl-terminal hydrolase 7 Functional site 1) chain A residue 218 type catalytic sequence N description 789 source MCSA : MCSA1 2) chain A residue 223 type catalytic sequence C description 789 source MCSA : MCSA1 3) chain A residue 464 type catalytic sequence H description 789 source MCSA : MCSA1 4) chain A residue 481 type catalytic sequence D description 789 source MCSA : MCSA1 5) chain B residue 218 type catalytic sequence N description 789 source MCSA : MCSA2 6) chain B residue 223 type catalytic sequence C description 789 source MCSA : MCSA2 7) chain B residue 464 type catalytic sequence H description 789 source MCSA : MCSA2 8) chain B residue 481 type catalytic sequence D description 789 source MCSA : MCSA2 9) chain E residue 218 type catalytic sequence N description 789 source MCSA : MCSA3 10) chain E residue 223 type catalytic sequence C description 789 source MCSA : MCSA3 11) chain E residue 464 type catalytic sequence H description 789 source MCSA : MCSA3 12) chain E residue 481 type catalytic sequence D description 789 source MCSA : MCSA3 13) chain C 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_FI3 14) chain D 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_FI3 15) chain C residue 366 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 16) chain D residue 366 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 17) chain C residue 376 type MOD_RES sequence X description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 18) chain D residue 376 type MOD_RES sequence X description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 19) chain C 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_FI6 20) chain D 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_FI6 21) chain C 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_FI12 22) chain D 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_FI12 23) chain C residue 354 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 24) chain C residue 372 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 25) chain D residue 354 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 26) chain D residue 372 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 27) chain C residue 368 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 28) chain D residue 368 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 29) chain E residue 464 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 30) chain C residue 327-352 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 31) chain A residue 215-230 type prosite sequence GLKNQGATCYMNSLLQ description USP_1 Ubiquitin specific protease (USP) domain signature 1. GLknqGAtCYMNSlLQ source prosite : PS00972 32) chain A residue 448-465 type prosite sequence YILHAVLVHSGDNHGGHY description USP_2 Ubiquitin specific protease (USP) domain signature 2. YiLhAVlvHsGdnhg..GHY source prosite : PS00973 33) chain C residue 376 type CROSSLNK sequence X description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 34) chain D residue 376 type CROSSLNK sequence X description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 35) chain C 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_FI8 36) chain C 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_FI8 37) chain D 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_FI8 38) chain D 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_FI8 39) chain C 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_FI10 40) chain D 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_FI10 41) chain C 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_FI11 42) chain D 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_FI11 43) chain C 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_FI9 44) chain D 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_FI9

Display surface Download Links