eF-site ID 4q66-ABCDEFGHIJKL PDB Code 4q66 Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title Structure of Exomer bound to Arf1. Classification PROTEIN TRANSPORT Compound Chs5p Source Saccharomyces cerevisiae R008 (ARF1_YEAST) Sequence A:  SSVDVLLTVGKLDASLALLTTQDHHVIEFPTVLLPENVKA GSIIKMQVSQNLEEEKKQRNHFKSIQAKILEKYGTHKPES PVLKIVNVTQTSCVLAWDPLKLGSAKLKSLILYRKGIRSM VIPNPFKVTTTKISGLSVDTPYEFQLKLITTSGTLWSEKV ILRTHKMTDMSGITVCLQRHVAIDTTHFVLIRAKHNNIPR PWVRACEVEKRIVGFYLDADQSTFPP B:  SQTSIPEVQRRARVGQFDLGPDLIFFYCMGIDTSDPTSIT IFASSWNAFRKYDVVNMIWAETFMSGIVRDIMIMKDNRAD GESQNLVETLIFNPFTLEDVANNFIKLFPLVYEKGVYLDA PTHVNPSLTNNYLVETLVEIVRLTKSLEACRKMLKKLIEI HPEAVIILIRVYFACDLEIDAVDLINEQLNSPSSFLSHIQ LIFKSELLSIQSEFLLDVKRDYKLAKEVAMEAVNCAPNEF KTWYLLTRIYIKLNDMSNALLSLNACPMSQVKEKYVLIAP ILHLPLPLDLEQKSDPNLVNLSASSLKSTFQLAYKLLTEI VQITGWEQLLKYRSKIFVKRLCERWLDNLFMLLYEDLKTY TDWQSEKLTVEWELFGLCAKRLGHLPEAAKAFQIGLSQRF SPVCAKNLLQFYIDEHKRIRRDSVSTSSQILSSINDIDSS IIDLVVKICCWNHRWYIEFIILIDALSVAVQDMGKVHNEI ASRFSDPVAQLIDDNILNFLKNFTNDT C:  ILMVGLDGAGKTTVLYKLKLGEVITTIPTIGFNVETVSFT VWDVGGLDRIRSLWRHYYRNTGVIFVVDSNDRSRIGEARE VMQLNEDELRVFANKQDLPEAMSAAEITEKLGWFIQATCA TSGEGLYEGLEWLS D:  VDVLLTVGKLDASLALLTTQDHHVIEFPTVLLPENVKAGS IIKMQVSQNLEEEKKQRNHFKSIQAKILEKYGTHKPESPV LKIVNVTQTSCVLAWDPLKLGSAKLKSLILYRRSMVIPNP FKVTTTKISGLVDTPYEFQLKLITTSGTLWSEKVILRTHK MTHVRGFYLDA E:  LSQTSIPEVKVIGYALHQRRARVGDLGPPDLIFFYCMGID TSDPTSITIFAKKITDLFLDTPQISISSWNAFRKYDVNII VVQTYIINSNVNMIWAETFMSGIVRDIMIMKDNRADGESQ NLVETLIFNPFTSGDVANNFIKLFPLVYEKGVYLDAPTHV LNPSLTNNYLVETLVEIVRLTKSLEACRKMLKKLIEIHPE AVIILIRVYFACDLEIDAVDLINEQLNSPSSFLADTSHIQ LIFKSELLSIQSEFLLDVKRDYKLAKEVAMEAVNCAPNEF KTWYLLTRIYIKLNDMSNALLSLNACPMSQVKEKYVLRAP ILHLPLPNPMDVQLEQKSADPNLVNLSASSLKSTFQLAYK LLTEIVQITGWEQLLKYRSKIFVSKRLCERWLDNLFMLLY EDLKTYTDWQSEQLKLTVEWELFGLCAKRLGHLPEAAKAF QIGLSQRFSPVCAKNLLQFYIDEHKRIRRDSTSSQILSSI NDIDSSIIDLVVKICCWNHRWYIEFSIILIDALSVAVQDM GITKVHNEIASRFSDPVAQLIDDNILNFLKNFTNDTF F:  MRILMVGLDGAGKTTVLYKLKPTIGFNVETVQYKFTVWDV GGLDRIRSLWRHYYRNTEGVIFVVDSNDRSRIGEAREVMQ RMLNEDELRNAAWLVFANKQDLPEAMSAAEITEKLGLHSI RPWFIQATCATSGEGLYEGLEWLSNS G:  SVDVLLTVGKLDASLALLTTQDHHVIEFPTVLLPENVKAG SIIKMQVSQNLEEEKKQRNHFKSIQAKILEKYGTPESPVL KIVNVTQTSCVLAWDPLKLAKLKSLILYRKGSMVIPNPFK VTTTKISGLSVDTPYEFQLKLITTSGTLWSEKVILRTHKM TDMSGITVSDLQISQCLSHIGAVAIDTTHFVELIRAKHNN IPIVRPEWVRA H:  VNMIWAETMSGIVRDIMIMKDNRADGESQNLNPFTSGKGV YLDAPTHVLNPSLTNNYLVETLEIVRLTKSLEACRKMLKL IEPEAVIILIRVYFACDLEIDAVDLINEQLTSHIQLIFKS ELLSIQSEFLLDVKRDYKLAKEVAMEAVNCAPNEFKTWYL LTRIYIKLNDMSNALLSLNACPMSQVKSTFQLAYKLLTEI VQITGWEQLLKYRSKIFVKRLCERWLDNLFMLLYEDLKTY TDWQSFGLCAKRLGPEAAKASPVCAKNLLQFYIDEHKRIR SSINDIDSSIIDLVVKICCWNHFSIILIDALSVAVQGITK VHNEIAPVAQLIILTNDT I:  LMVGLDGAKTTVLYKLKLGVITTIPTGGLDRIRSLWRHYY VIFVVDSNREVMQRMLVFANKQDAAEITEKLGLATCATSG EGLYEG J:  VDVLLTVGKLDASLALLTTQDHHVIEFPTVLLPENVKAGS IIKMQVSQNLEEEKKQRNHFKSIQAKILEKYGTHKPESPV LIVNVTSCVLAWDPLKLGSAKLKSLILYRKGIRSMVIPNP FKVTTTKISGLSVDTEFQLKLITTSGTLWSEKVILRTH K:  SQTSIPEVKEDVIGYALHQRRARVGQFQDLGPPDLIFFYC MGIDTSDPTSITIFAKKITDLFLDTPQIWFGKKHFHVSKI SISSWNAFRKYDVNIIVHVQTYIINSDGEQSQLPSVLNVN MIWAETFMSGIVRDIMIMKDNRADGESQNLVETLIFNPFT SGELEDVANNFIKLFPLVYEKGVYLDAPTHVLNPSLTNNY LVETLVEIVRLTKSLEACRKMLKKLIEIHPEAVIILIRVY FACDLEDAVDLINEQLNSPSSFLADTSHIQLIFKSELLSI QSEFLLDVKRDYKLAKEVAMEAVNCAPNEFKTWYLLTRIY IKLNDMSNALLSLNACPMSVKEKYVLRRIAPIENLHLPLP LDNPMDVQLEQKSADPNLVNLSASSLKSTFQLAYKLLTEI VQITGWEQLLKYRSKIFVMSKRLCERWLDNLFMLLYEDLK TYTDWQSEQLYFDAHKLTVEWELFGLCAKRLGHLPEAAKA FQIGLSQRFSPVCAKNLLQFYIDEHKRIRRDSLSSINDID SSIIDLVVKICCWNHRWYIEFSIILIDALSVAVQDMGITK VHNEIASRFSDPVAQLIDDNILNFLKNFTNDTF L:  MRILMVGLDGAGKTTVLYKLKLGTTIPTIGFNVETVFTVW DVGGLDRIRSLWRHYYRNTEGVIFVVDSNDRSRIGEAREV MQRMLNEDELRNAAWLVFANKEAMSAAEITEKLLHSIRPW FIQATCAGLYEGLEWLSNS Description Functional site 1) chain F residue 26 type sequence D description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 2) chain F residue 27 type sequence G description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 3) chain F residue 28 type sequence A description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 4) chain F residue 29 type sequence G description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 5) chain F residue 30 type sequence K description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 6) chain F residue 31 type sequence T description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 7) chain F residue 32 type sequence T description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 8) chain F residue 47 type sequence P description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 9) chain F residue 48 type sequence T description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 10) chain F residue 70 type sequence G description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 11) chain F residue 126 type sequence N description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 12) chain F residue 127 type sequence K description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 13) chain F residue 129 type sequence D description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 14) chain F residue 130 type sequence L description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 15) chain F residue 159 type sequence C description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 16) chain F residue 160 type sequence A description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 17) chain F residue 161 type sequence T description BINDING SITE FOR RESIDUE GNP F 201 source : AC1 18) chain F residue 31 type sequence T description BINDING SITE FOR RESIDUE MG F 202 source : AC2 19) chain F residue 48 type sequence T description BINDING SITE FOR RESIDUE MG F 202 source : AC2 20) chain F residue 67 type sequence D description BINDING SITE FOR RESIDUE MG F 202 source : AC2 21) chain L residue 25 type sequence L description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 22) chain L residue 26 type sequence D description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 23) chain L residue 27 type sequence G description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 24) chain L residue 28 type sequence A description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 25) chain L residue 29 type sequence G description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 26) chain L residue 30 type sequence K description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 27) chain L residue 31 type sequence T description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 28) chain L residue 32 type sequence T description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 29) chain L residue 45 type sequence T description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 30) chain L residue 46 type sequence I description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 31) chain L residue 47 type sequence P description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 32) chain L residue 48 type sequence T description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 33) chain L residue 70 type sequence G description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 34) chain L residue 126 type sequence N description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 35) chain L residue 127 type sequence K description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 36) chain L residue 159 type sequence C description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 37) chain L residue 160 type sequence A description BINDING SITE FOR RESIDUE GNP L 201 source : AC3 38) chain L residue 31 type sequence T description BINDING SITE FOR RESIDUE MG L 202 source : AC4 39) chain L residue 48 type sequence T description BINDING SITE FOR RESIDUE MG L 202 source : AC4 40) chain C residue 25 type sequence L description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 41) chain C residue 26 type sequence D description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 42) chain C residue 27 type sequence G description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 43) chain C residue 28 type sequence A description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 44) chain C residue 29 type sequence G description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 45) chain C residue 30 type sequence K description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 46) chain C residue 31 type sequence T description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 47) chain C residue 32 type sequence T description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 48) chain C residue 45 type sequence T description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 49) chain C residue 46 type sequence I description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 50) chain C residue 47 type sequence P description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 51) chain C residue 48 type sequence T description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 52) chain C residue 70 type sequence G description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 53) chain C residue 126 type sequence N description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 54) chain C residue 127 type sequence K description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 55) chain C residue 129 type sequence D description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 56) chain C residue 159 type sequence C description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 57) chain C residue 160 type sequence A description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 58) chain C residue 161 type sequence T description BINDING SITE FOR RESIDUE GNP C 201 source : AC5 59) chain C residue 31 type sequence T description BINDING SITE FOR RESIDUE MG C 202 source : AC6 60) chain C residue 48 type sequence T description BINDING SITE FOR RESIDUE MG C 202 source : AC6 61) chain I residue 25 type sequence L description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 62) chain I residue 26 type sequence D description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 63) chain I residue 27 type sequence G description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 64) chain I residue 28 type sequence A description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 65) chain I residue 30 type sequence K description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 66) chain I residue 31 type sequence T description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 67) chain I residue 32 type sequence T description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 68) chain I residue 45 type sequence T description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 69) chain I residue 47 type sequence P description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 70) chain I residue 48 type sequence T description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 71) chain I residue 70 type sequence G description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 72) chain I residue 126 type sequence N description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 73) chain I residue 127 type sequence K description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 74) chain I residue 129 type sequence D description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 75) chain I residue 159 type sequence C description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 76) chain I residue 160 type sequence A description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 77) chain I residue 161 type sequence T description BINDING SITE FOR RESIDUE GNP I 201 source : AC7 78) chain I residue 31 type sequence T description BINDING SITE FOR RESIDUE MG I 202 source : AC8 79) chain I residue 48 type sequence T description BINDING SITE FOR RESIDUE MG I 202 source : AC8 80) chain C residue 70 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 81) chain C residue 126 type BINDING sequence N description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 82) chain C residue 160 type BINDING sequence A description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 83) chain I residue 25 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 84) chain I residue 48 type BINDING sequence T description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 85) chain I residue 70 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 86) chain I residue 126 type BINDING sequence N description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 87) chain I residue 160 type BINDING sequence A description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 88) chain F residue 25 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 89) chain F residue 48 type BINDING sequence T description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 90) chain F residue 70 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 91) chain F residue 126 type BINDING sequence N description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 92) chain F residue 160 type BINDING sequence A description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 93) chain L residue 25 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 94) chain L residue 48 type BINDING sequence T description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 95) chain L residue 70 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 96) chain L residue 126 type BINDING sequence N description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 97) chain L residue 160 type BINDING sequence A description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 98) chain C residue 25 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 99) chain C residue 48 type BINDING sequence T description BINDING => ECO:0000269|PubMed:20601958 source Swiss-Prot : SWS_FT_FI1 100) chain C residue 127 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI2 101) chain I residue 127 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI2 102) chain F residue 127 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI2 103) chain L residue 127 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI2

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