eF-site ID 3j95-ABCDEF PDB Code 3j95 Chain A, B, C, D, E, F Title Structure of ADP-bound N-ethylmaleimide sensitive factor determined by single particle cryoelectron microscopy Classification HYDROLASE Compound Vesicle-fusing ATPase Source (NSF_CRIGR) Sequence A:  FEKMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVK GILLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKY VGESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAIC HDTVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRP GRLEVKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDI KELAVETKNFSGAELEGLVRAAQSTAMNRHIDFLASLEND IKEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRT PLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMI GFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPI GPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQE MEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTI AQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLR EEG B:  KMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGI LLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVG ESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIHDTVVN QLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVK MEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVE TKNFSGAELEGLVRAAQSTAMNRHIDFLASLENDIKPAFG EDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPL VSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGF SETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIGP RFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEME MLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIAQ QVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLREE G C:  KMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGI LLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVG ESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICHD TVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGR LEVKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKE LAVETKNFSGAELEGLVRAAQSTAMNRHIDFLASLENDIK PAFGEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSD RTPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDK MIGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYV PIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVL QEMEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERT TIAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLAL LREEG D:  KMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGI LLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVG ESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAIDTV VNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLE VKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELA VETKNFSGAELEGLVRAAQSTAMNRHIFLASLENDIKPED YASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVS VLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGFSE TAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRF SNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEML NAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIAQQV KGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLREEG E:  KMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGI LLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVG ESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIHDTVVN QLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVK MEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVE TKNFSGAELEGLVRAAQSTAMNRHIDFLASLENDIKPAFG TEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTP LVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIG FSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIG PRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEM EMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIA QQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLRE EG F:  GIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGILL YGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVGES EANIRKLFADAEEEQRRLGANSGLHIIIFDEIHDTVVNQL LSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVKME IGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVETK NFSGAELEGLVRAAQSTAMNRHIDFLASLENDIKPASYIM NGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGP PHSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQA MKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQ ALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTT IHVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVW IGIKKLLMLIEMSLQMDPEYRVRKFLALLREEG Description Functional site 1) chain B residue 502 type sequence Y description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 2) chain B residue 503 type sequence I description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 3) chain B residue 504 type sequence M description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 4) chain B residue 505 type sequence N description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 5) chain B residue 506 type sequence G description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 6) chain B residue 507 type sequence I description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 7) chain B residue 508 type sequence I description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 8) chain B residue 510 type sequence W description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 9) chain B residue 546 type sequence H description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 10) chain B residue 547 type sequence S description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 11) chain B residue 548 type sequence G description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 12) chain B residue 549 type sequence K description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 13) chain B residue 550 type sequence T description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 14) chain B residue 551 type sequence A description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 15) chain B residue 552 type sequence L description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 16) chain B residue 707 type sequence I description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 17) chain B residue 708 type sequence K description BINDING SITE FOR RESIDUE ADP B 801 source : AC1 18) chain C residue 503 type sequence I description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 19) chain C residue 504 type sequence M description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 20) chain C residue 505 type sequence N description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 21) chain C residue 506 type sequence G description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 22) chain C residue 507 type sequence I description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 23) chain C residue 508 type sequence I description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 24) chain C residue 510 type sequence W description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 25) chain C residue 514 type sequence V description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 26) chain C residue 548 type sequence G description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 27) chain C residue 549 type sequence K description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 28) chain C residue 550 type sequence T description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 29) chain C residue 551 type sequence A description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 30) chain C residue 708 type sequence K description BINDING SITE FOR RESIDUE ADP C 801 source : AC2 31) chain D residue 502 type sequence Y description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 32) chain D residue 503 type sequence I description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 33) chain D residue 504 type sequence M description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 34) chain D residue 506 type sequence G description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 35) chain D residue 507 type sequence I description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 36) chain D residue 508 type sequence I description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 37) chain D residue 514 type sequence V description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 38) chain D residue 546 type sequence H description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 39) chain D residue 547 type sequence S description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 40) chain D residue 548 type sequence G description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 41) chain D residue 549 type sequence K description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 42) chain D residue 550 type sequence T description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 43) chain D residue 551 type sequence A description BINDING SITE FOR RESIDUE ADP D 801 source : AC3 44) chain E residue 505 type sequence N description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 45) chain E residue 506 type sequence G description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 46) chain E residue 507 type sequence I description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 47) chain E residue 510 type sequence W description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 48) chain E residue 514 type sequence V description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 49) chain E residue 546 type sequence H description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 50) chain E residue 547 type sequence S description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 51) chain E residue 548 type sequence G description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 52) chain E residue 549 type sequence K description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 53) chain E residue 550 type sequence T description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 54) chain E residue 551 type sequence A description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 55) chain E residue 552 type sequence L description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 56) chain E residue 707 type sequence I description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 57) chain E residue 708 type sequence K description BINDING SITE FOR RESIDUE ADP E 801 source : AC4 58) chain A residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 59) chain A residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 60) chain B residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 61) chain B residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 62) chain C residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 63) chain C residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 64) chain D residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 65) chain D residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 66) chain E residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 67) chain E residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 68) chain F residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 69) chain F residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 70) chain A residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 71) chain B residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 72) chain C residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 73) chain D residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 74) chain E residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 75) chain F residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 76) chain A residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 77) chain B residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 78) chain C residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 79) chain D residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 80) chain E residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 81) chain F residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 82) chain A residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 83) chain B residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 84) chain C residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 85) chain D residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 86) chain E residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 87) chain F residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 88) chain A residue 367-385 type prosite sequence ILVIGMTNRPDLIDEALLR description AAA AAA-protein family signature. IlVIgMTNrpdlIDeALl.R source prosite : PS00674 89) chain A residue 549 type catalytic sequence K description 642 source MCSA : MCSA1 90) chain A residue 550 type catalytic sequence T description 642 source MCSA : MCSA1 91) chain A residue 603 type catalytic sequence D description 642 source MCSA : MCSA1 92) chain A residue 604 type catalytic sequence D description 642 source MCSA : MCSA1 93) chain A residue 631 type catalytic sequence K description 642 source MCSA : MCSA1 94) chain A residue 708 type catalytic sequence K description 642 source MCSA : MCSA1 95) chain B residue 549 type catalytic sequence K description 642 source MCSA : MCSA2 96) chain B residue 550 type catalytic sequence T description 642 source MCSA : MCSA2 97) chain B residue 603 type catalytic sequence D description 642 source MCSA : MCSA2 98) chain B residue 604 type catalytic sequence D description 642 source MCSA : MCSA2 99) chain B residue 631 type catalytic sequence K description 642 source MCSA : MCSA2 100) chain B residue 708 type catalytic sequence K description 642 source MCSA : MCSA2 101) chain C residue 549 type catalytic sequence K description 642 source MCSA : MCSA3 102) chain C residue 550 type catalytic sequence T description 642 source MCSA : MCSA3 103) chain C residue 603 type catalytic sequence D description 642 source MCSA : MCSA3 104) chain C residue 604 type catalytic sequence D description 642 source MCSA : MCSA3 105) chain C residue 631 type catalytic sequence K description 642 source MCSA : MCSA3 106) chain C residue 708 type catalytic sequence K description 642 source MCSA : MCSA3 107) chain D residue 549 type catalytic sequence K description 642 source MCSA : MCSA4 108) chain D residue 550 type catalytic sequence T description 642 source MCSA : MCSA4 109) chain D residue 603 type catalytic sequence D description 642 source MCSA : MCSA4 110) chain D residue 604 type catalytic sequence D description 642 source MCSA : MCSA4 111) chain D residue 631 type catalytic sequence K description 642 source MCSA : MCSA4 112) chain D residue 708 type catalytic sequence K description 642 source MCSA : MCSA4 113) chain E residue 549 type catalytic sequence K description 642 source MCSA : MCSA5 114) chain E residue 550 type catalytic sequence T description 642 source MCSA : MCSA5 115) chain E residue 603 type catalytic sequence D description 642 source MCSA : MCSA5 116) chain E residue 604 type catalytic sequence D description 642 source MCSA : MCSA5 117) chain E residue 631 type catalytic sequence K description 642 source MCSA : MCSA5 118) chain E residue 708 type catalytic sequence K description 642 source MCSA : MCSA5 119) chain F residue 549 type catalytic sequence K description 642 source MCSA : MCSA6 120) chain F residue 550 type catalytic sequence T description 642 source MCSA : MCSA6 121) chain F residue 603 type catalytic sequence D description 642 source MCSA : MCSA6 122) chain F residue 604 type catalytic sequence D description 642 source MCSA : MCSA6 123) chain F residue 631 type catalytic sequence K description 642 source MCSA : MCSA6 124) chain F residue 708 type catalytic sequence K description 642 source MCSA : MCSA6

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