eF-site ID 4nql-ABC PDB Code 4nql Chain A, B, C click to enlarge Title The crystal structure of the DUB domain of AMSH orthologue, Sst2 from S. pombe, in complex with lysine 63-linked diubiquitin Classification HYDROLASE/PROTEIN BINDING Compound AMSH-like protease sst2 Source Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (UBC_MOUSE) Sequence A:  FKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLAT CGILCGKLRQNAFFITHLVIPLQEATSDTCGTTDEASLFE FQDKHNLLTLGWIHTHPTQTCFMSSVALHTHCSYQLMLPE AIAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLFHPHE GKVYTMVAQPGHVREINSKLQVVDLRV B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQRESTLHLVLRLRGG C:  MQIFVKTITLEVEPSDTIENVKLIFAKQLEDGRTLSDYNI QKESTLHL Description Functional site 1) chain A residue 356 type sequence H description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 2) chain A residue 397 type sequence C description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 3) chain A residue 404 type sequence H description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 4) chain A residue 406 type sequence H description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 5) chain A residue 325 type sequence L description BINDING SITE FOR RESIDUE EDO A 502 source : AC2 6) chain A residue 329 type sequence Q description BINDING SITE FOR RESIDUE EDO A 502 source : AC2 7) chain A residue 336 type sequence T description BINDING SITE FOR RESIDUE EDO A 502 source : AC2 8) chain A residue 361 type sequence Y description BINDING SITE FOR RESIDUE EDO A 502 source : AC2 9) chain B residue 8 type sequence L description BINDING SITE FOR RESIDUE EDO A 502 source : AC2 10) chain B residue 71 type sequence L description BINDING SITE FOR RESIDUE EDO A 502 source : AC2 11) chain A residue 284 type sequence N description BINDING SITE FOR RESIDUE EDO A 503 source : AC3 12) chain A residue 314 type sequence S description BINDING SITE FOR RESIDUE EDO A 503 source : AC3 13) chain A residue 315 type sequence D description BINDING SITE FOR RESIDUE EDO A 503 source : AC3 14) chain A residue 345 type sequence T description BINDING SITE FOR RESIDUE EDO A 503 source : AC3 15) chain A residue 316 type sequence T description BINDING SITE FOR RESIDUE EDO A 504 source : AC4 16) chain A residue 317 type sequence C description BINDING SITE FOR RESIDUE EDO A 504 source : AC4 17) chain A residue 318 type sequence G description BINDING SITE FOR RESIDUE EDO A 504 source : AC4 18) chain B residue 22 type sequence T description BINDING SITE FOR RESIDUE EDO A 504 source : AC4 19) chain B residue 53 type sequence G description BINDING SITE FOR RESIDUE EDO A 504 source : AC4 20) chain B residue 74 type sequence R description BINDING SITE FOR RESIDUE EDO A 504 source : AC4 21) chain A residue 381 type sequence G description BINDING SITE FOR RESIDUE EDO A 505 source : AC5 22) chain A residue 382 type sequence I description BINDING SITE FOR RESIDUE EDO A 505 source : AC5 23) chain A residue 413 type sequence M description BINDING SITE FOR RESIDUE EDO A 505 source : AC5 24) chain A residue 414 type sequence V description BINDING SITE FOR RESIDUE EDO A 505 source : AC5 25) chain A residue 416 type sequence Q description BINDING SITE FOR RESIDUE EDO A 505 source : AC5 26) chain A residue 258 type sequence K description BINDING SITE FOR RESIDUE EDO A 506 source : AC6 27) chain A residue 362 type sequence Q description BINDING SITE FOR RESIDUE EDO A 506 source : AC6 28) chain A residue 366 type sequence P description BINDING SITE FOR RESIDUE EDO A 506 source : AC6 29) chain A residue 387 type sequence D description BINDING SITE FOR RESIDUE EDO A 506 source : AC6 30) chain B residue 7 type sequence T description BINDING SITE FOR RESIDUE EDO B 101 source : AC7 31) chain B residue 8 type sequence L description BINDING SITE FOR RESIDUE EDO B 101 source : AC7 32) chain B residue 69 type sequence L description BINDING SITE FOR RESIDUE EDO B 101 source : AC7 33) chain B residue 70 type sequence V description BINDING SITE FOR RESIDUE EDO B 101 source : AC7 34) chain B residue 71 type sequence L description BINDING SITE FOR RESIDUE EDO B 101 source : AC7 35) chain A residue 349 type sequence F description BINDING SITE FOR RESIDUE EDO C 101 source : AC8 36) chain C residue 62 type sequence Q description BINDING SITE FOR RESIDUE EDO C 101 source : AC8 37) chain C residue 63 type sequence K description BINDING SITE FOR RESIDUE EDO C 101 source : AC8 38) chain C residue 64 type sequence E description BINDING SITE FOR RESIDUE EDO C 101 source : AC8 39) chain C residue 65 type sequence S description BINDING SITE FOR RESIDUE EDO C 101 source : AC8 40) chain C residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 41) chain C residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 42) chain C residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 43) chain C residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 44) chain C residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 45) chain A residue 354 type SITE sequence A description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 46) chain C residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 47) chain A residue 397 type SITE sequence C description Essential for function source Swiss-Prot : SWS_FT_FI2 48) chain A residue 404 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 49) chain A residue 406 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 50) chain C residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI3 51) chain B residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 52) chain C residue 27-52 type prosite sequence KLIFAKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299

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