eF-site ID 4zft-ABCD PDB Code 4zft Chain A, B, C, D click to enlarge Title Catalytic domain of Sst2 F403W mutant bound to ubiquitin Classification HYDROLASE Compound AMSH-like protease sst2 Source (UBB_HUMAN) Sequence A:  KIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETC GILCGKLRQNAFFITHLVIPLQEATSDTCGTTDEASLFEF QDKHNLLTLGWIHTHPTQTCFMSSVDLHTHCSYQLMLPEA IAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLWHPHEG KVYTMVAQPGHVREINSKLQVVDLR B:  GSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPP DQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG C:  HAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETCGI LCGKLRQNAFFITHLVIPLQEATSDTCGTTDEASLFEFQD KHNLLTLGWIHTHPTQTCFMSSVDLHTHCSYQLMLPEAIA IVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLWHPHEGKV YTMVAQPGHVREINSKLQVVDLR D:  SMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG Description Functional site 1) chain A residue 341 type sequence H description binding site for residue ZN A 501 source : AC1 2) chain A residue 343 type sequence H description binding site for residue ZN A 501 source : AC1 3) chain A residue 354 type sequence D description binding site for residue ZN A 501 source : AC1 4) chain B residue 76 type sequence G description binding site for residue ZN A 501 source : AC1 5) chain A residue 356 type sequence H description binding site for residue ZN A 502 source : AC2 6) chain A residue 397 type sequence C description binding site for residue ZN A 502 source : AC2 7) chain A residue 404 type sequence H description binding site for residue ZN A 502 source : AC2 8) chain A residue 406 type sequence H description binding site for residue ZN A 502 source : AC2 9) chain A residue 252 type sequence A description binding site for residue EDO A 503 source : AC3 10) chain A residue 253 type sequence Y description binding site for residue EDO A 503 source : AC3 11) chain A residue 260 type sequence L description binding site for residue EDO A 503 source : AC3 12) chain A residue 384 type sequence R description binding site for residue EDO A 503 source : AC3 13) chain A residue 414 type sequence V description binding site for residue EDO A 503 source : AC3 14) chain A residue 415 type sequence A description binding site for residue EDO A 503 source : AC3 15) chain A residue 419 type sequence H description binding site for residue EDO A 503 source : AC3 16) chain A residue 426 type sequence K description binding site for residue EDO A 503 source : AC3 17) chain B residue 7 type sequence T description binding site for residue EDO B 101 source : AC4 18) chain B residue 8 type sequence L description binding site for residue EDO B 101 source : AC4 19) chain B residue 69 type sequence L description binding site for residue EDO B 101 source : AC4 20) chain B residue 70 type sequence V description binding site for residue EDO B 101 source : AC4 21) chain B residue 71 type sequence L description binding site for residue EDO B 101 source : AC4 22) chain A residue 334 type sequence L description binding site for residue EDO B 102 source : AC5 23) chain B residue 7 type sequence T description binding site for residue EDO B 102 source : AC5 24) chain B residue 8 type sequence L description binding site for residue EDO B 102 source : AC5 25) chain B residue 9 type sequence T description binding site for residue EDO B 102 source : AC5 26) chain B residue 10 type sequence G description binding site for residue EDO B 102 source : AC5 27) chain C residue 341 type sequence H description binding site for residue ZN C 501 source : AC6 28) chain C residue 343 type sequence H description binding site for residue ZN C 501 source : AC6 29) chain C residue 354 type sequence D description binding site for residue ZN C 501 source : AC6 30) chain D residue 76 type sequence G description binding site for residue ZN C 501 source : AC6 31) chain C residue 356 type sequence H description binding site for residue ZN C 502 source : AC7 32) chain C residue 397 type sequence C description binding site for residue ZN C 502 source : AC7 33) chain C residue 404 type sequence H description binding site for residue ZN C 502 source : AC7 34) chain C residue 406 type sequence H description binding site for residue ZN C 502 source : AC7 35) chain C residue 264 type sequence Y description binding site for residue EDO C 503 source : AC8 36) chain D residue 7 type sequence T description binding site for residue EDO D 101 source : AC9 37) chain D residue 8 type sequence L description binding site for residue EDO D 101 source : AC9 38) chain D residue 69 type sequence L description binding site for residue EDO D 101 source : AC9 39) chain D residue 70 type sequence V description binding site for residue EDO D 101 source : AC9 40) chain D residue 71 type sequence L description binding site for residue EDO D 101 source : AC9 41) chain A residue 341 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01182 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 343 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01182 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 354 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01182 source Swiss-Prot : SWS_FT_FI1 44) chain C residue 341 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01182 source Swiss-Prot : SWS_FT_FI1 45) chain C residue 343 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01182 source Swiss-Prot : SWS_FT_FI1 46) chain C residue 354 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01182 source Swiss-Prot : SWS_FT_FI1 47) chain A residue 356 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 397 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 404 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 406 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 51) chain C residue 356 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 52) chain C residue 397 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 53) chain C residue 404 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 54) chain C residue 406 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 286 type SITE sequence E description Indirect zinc-binding => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 56) chain C residue 286 type SITE sequence E description Indirect zinc-binding => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 57) chain B residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299

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