eF-site ID 6o7r-ABCD PDB Code 6o7r Chain A, B, C, D click to enlarge Title Nitrogenase MoFeP mutant F99Y, S188A from Azotobacter vinelandii in the dithionite reduced state Classification OXIDOREDUCTASE Compound Nitrogenase molybdenum-iron protein alpha chain Source ORGANISM_SCIENTIFIC: Azotobacter vinelandii; Sequence A:  SREEVESLIQEVLEVYPEKARKDRNKHLAVNDPAVTQSKK CIISNKKSQPGLMTIRGCAYAGSKGVVWGPIKDMIHISHG PVGCGQYSRAGRRNYYIGTTGVNAFVTMNFTSDFQEKDIV FGGDKKLAKLIDEVETLFPLNKGISVQSECPIGLIGDDIE SVSKVKGAELSKTIVPVRCEGFRGVSQSLGHHIANDAVRD WVLGKRDEDTTFASTPYDVAIIGDYNIGGDAWSSRILLEE MGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISR HMEEKYGIPWMEYNFFGPTKTIESLRAIAAKFDESIQKKC EEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVI GAYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDV TGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREMHSW DYSGPYHGFDGFAIFARDMDMTLNNPCWKKLQAPWE B:  SQQVDKIKASYPLFLDQDYKDMLAKKRDGFEEKYPQDKID EVFQWTTTKEYQELNFQREALTVNPAKACQPLGAVLCALG FEKTMPYVHGSQGCVAYYRSYFNRHFREPVSCVSDSMTED AAVFGGQQNMKDGLQNCKATYKPDMIAVSTTCMAEVIGDD LNAFINNSKKEGFIPDEFPVPFAHTPAFVGSHVTGWDNMF EGIARYFTLKSMDDKVVGSNKKINIVPGFETYLGNFRVIK RMLSEMGVGYSLLSDPEEVLDTPADGQFRMYAGGTTQEEM KDAPNALNTVLLQPWHLEKTKKFVEGTWKHEVPKLNIPMG LDWTDEFLMKVSEISGQPIPASLTKERGRLVDMMTDSHTW LHGKRFALWGDPDFVMGLVKFLLELGCEPVHILCHNGNKR WKKAVDAILAASPYGKNATVYIGKDLWHLRSLVFTDKPDF MIGNSYGKFIQRDTLHKGKEFEVPLIRIGFPIFDRHHLHR STTLGYEGAMQILTTLVNSILERLDEETRGMQATDYNHDL VR C:  MSREEVESLIQEVLEVYPEKARKDRNKHLAVNDPAVTQSK KCIISNKKSQPGLMTIRGCAYAGSKGVVWGPIKDMIHISH GPVGCGQYSRAGRRNYYIGTTGVNAFVTMNFTSDFQEKDI VFGGDKKLAKLIDEVETLFPLNKGISVQSECPIGLIGDDI ESVSKVKGAELSKTIVPVRCEGFRGVSQSLGHHIANDAVR DWVLGKRDEDTTFASTPYDVAIIGDYNIGGDAWSSRILLE EMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYIS RHMEEKYGIPWMEYNFFGPTKTIESLRAIAAKFDESIQKK CEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHV IGAYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDD VTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREMHS WDYSGPYHGFDGFAIFARDMDMTLNNPCWKKLQAPWEA D:  SQQVDKIKASYPLFLDQDYKDMLAKKRDGFEEKYPQDKID EVFQWTTTKEYQELNFQREALTVNPAKACQPLGAVLCALG FEKTMPYVHGSQGCVAYYRSYFNRHFREPVSCVSDSMTED AAVFGGQQNMKDGLQNCKATYKPDMIAVSTTCMAEVIGDD LNAFINNSKKEGFIPDEFPVPFAHTPAFVGSHVTGWDNMF EGIARYFTLKSMDDKVVGSNKKINIVPGFETYLGNFRVIK RMLSEMGVGYSLLSDPEEVLDTPADGQFRMYAGGTTQEEM KDAPNALNTVLLQPWHLEKTKKFVEGTWKHEVPKLNIPMG LDWTDEFLMKVSEISGQPIPASLTKERGRLVDMMTDSHTW LHGKRFALWGDPDFVMGLVKFLLELGCEPVHILCHNGNKR WKKAVDAILAASPYGKNATVYIGKDLWHLRSLVFTDKPDF MIGNSYGKFIQRDTLHKGKEFEVPLIRIGFPIFDRHHLHR STTLGYEGAMQILTTLVNSILERLDEETRGMQATDYNHDL VR Description Functional site 1) chain A residue 65 type sequence A description binding site for residue HCA A 501 source : AC1 2) chain A residue 96 type sequence R description binding site for residue HCA A 501 source : AC1 3) chain A residue 191 type sequence Q description binding site for residue HCA A 501 source : AC1 4) chain A residue 424 type sequence G description binding site for residue HCA A 501 source : AC1 5) chain A residue 425 type sequence I description binding site for residue HCA A 501 source : AC1 6) chain A residue 442 type sequence H description binding site for residue HCA A 501 source : AC1 7) chain A residue 70 type sequence V description binding site for residue ICS A 502 source : AC2 8) chain A residue 96 type sequence R description binding site for residue ICS A 502 source : AC2 9) chain A residue 195 type sequence H description binding site for residue ICS A 502 source : AC2 10) chain A residue 229 type sequence Y description binding site for residue ICS A 502 source : AC2 11) chain A residue 275 type sequence C description binding site for residue ICS A 502 source : AC2 12) chain A residue 278 type sequence S description binding site for residue ICS A 502 source : AC2 13) chain A residue 355 type sequence I description binding site for residue ICS A 502 source : AC2 14) chain A residue 356 type sequence G description binding site for residue ICS A 502 source : AC2 15) chain A residue 357 type sequence G description binding site for residue ICS A 502 source : AC2 16) chain A residue 358 type sequence L description binding site for residue ICS A 502 source : AC2 17) chain A residue 359 type sequence R description binding site for residue ICS A 502 source : AC2 18) chain A residue 381 type sequence F description binding site for residue ICS A 502 source : AC2 19) chain A residue 442 type sequence H description binding site for residue ICS A 502 source : AC2 20) chain A residue 62 type sequence C description binding site for residue CLF B 601 source : AC3 21) chain A residue 64 type sequence Y description binding site for residue CLF B 601 source : AC3 22) chain A residue 85 type sequence P description binding site for residue CLF B 601 source : AC3 23) chain A residue 88 type sequence C description binding site for residue CLF B 601 source : AC3 24) chain A residue 154 type sequence C description binding site for residue CLF B 601 source : AC3 25) chain A residue 185 type sequence G description binding site for residue CLF B 601 source : AC3 26) chain B residue 70 type sequence C description binding site for residue CLF B 601 source : AC3 27) chain B residue 92 type sequence S description binding site for residue CLF B 601 source : AC3 28) chain B residue 95 type sequence C description binding site for residue CLF B 601 source : AC3 29) chain B residue 98 type sequence Y description binding site for residue CLF B 601 source : AC3 30) chain B residue 99 type sequence Y description binding site for residue CLF B 601 source : AC3 31) chain B residue 153 type sequence C description binding site for residue CLF B 601 source : AC3 32) chain B residue 188 type sequence A description binding site for residue CLF B 601 source : AC3 33) chain B residue 353 type sequence D description binding site for residue FE B 602 source : AC4 34) chain B residue 357 type sequence D description binding site for residue FE B 602 source : AC4 35) chain D residue 108 type sequence R description binding site for residue FE B 602 source : AC4 36) chain D residue 109 type sequence E description binding site for residue FE B 602 source : AC4 37) chain C residue 65 type sequence A description binding site for residue HCA C 501 source : AC5 38) chain C residue 96 type sequence R description binding site for residue HCA C 501 source : AC5 39) chain C residue 191 type sequence Q description binding site for residue HCA C 501 source : AC5 40) chain C residue 424 type sequence G description binding site for residue HCA C 501 source : AC5 41) chain C residue 425 type sequence I description binding site for residue HCA C 501 source : AC5 42) chain C residue 442 type sequence H description binding site for residue HCA C 501 source : AC5 43) chain C residue 96 type sequence R description binding site for residue ICS C 502 source : AC6 44) chain C residue 195 type sequence H description binding site for residue ICS C 502 source : AC6 45) chain C residue 229 type sequence Y description binding site for residue ICS C 502 source : AC6 46) chain C residue 275 type sequence C description binding site for residue ICS C 502 source : AC6 47) chain C residue 355 type sequence I description binding site for residue ICS C 502 source : AC6 48) chain C residue 356 type sequence G description binding site for residue ICS C 502 source : AC6 49) chain C residue 357 type sequence G description binding site for residue ICS C 502 source : AC6 50) chain C residue 359 type sequence R description binding site for residue ICS C 502 source : AC6 51) chain C residue 381 type sequence F description binding site for residue ICS C 502 source : AC6 52) chain C residue 442 type sequence H description binding site for residue ICS C 502 source : AC6 53) chain C residue 62 type sequence C description binding site for residue CLF D 601 source : AC7 54) chain C residue 64 type sequence Y description binding site for residue CLF D 601 source : AC7 55) chain C residue 85 type sequence P description binding site for residue CLF D 601 source : AC7 56) chain C residue 87 type sequence G description binding site for residue CLF D 601 source : AC7 57) chain C residue 88 type sequence C description binding site for residue CLF D 601 source : AC7 58) chain C residue 154 type sequence C description binding site for residue CLF D 601 source : AC7 59) chain C residue 185 type sequence G description binding site for residue CLF D 601 source : AC7 60) chain D residue 70 type sequence C description binding site for residue CLF D 601 source : AC7 61) chain D residue 92 type sequence S description binding site for residue CLF D 601 source : AC7 62) chain D residue 95 type sequence C description binding site for residue CLF D 601 source : AC7 63) chain D residue 98 type sequence Y description binding site for residue CLF D 601 source : AC7 64) chain D residue 99 type sequence Y description binding site for residue CLF D 601 source : AC7 65) chain D residue 153 type sequence C description binding site for residue CLF D 601 source : AC7 66) chain D residue 188 type sequence A description binding site for residue CLF D 601 source : AC7 67) chain B residue 108 type sequence R description binding site for residue FE D 602 source : AC8 68) chain B residue 109 type sequence E description binding site for residue FE D 602 source : AC8 69) chain D residue 353 type sequence D description binding site for residue FE D 602 source : AC8 70) chain D residue 357 type sequence D description binding site for residue FE D 602 source : AC8 71) chain B residue 153 type catalytic sequence C description 212 source MCSA : MCSA1 72) chain B residue 157 type catalytic sequence V description 212 source MCSA : MCSA1 73) chain A residue 96 type catalytic sequence R description 212 source MCSA : MCSA1 74) chain A residue 195 type catalytic sequence H description 212 source MCSA : MCSA1 75) chain D residue 153 type catalytic sequence C description 212 source MCSA : MCSA2 76) chain D residue 157 type catalytic sequence V description 212 source MCSA : MCSA2 77) chain C residue 96 type catalytic sequence R description 212 source MCSA : MCSA2 78) chain C residue 195 type catalytic sequence H description 212 source MCSA : MCSA2 79) chain B residue 70 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 80) chain C residue 442 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 81) chain B residue 95 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 82) chain B residue 153 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 83) chain B residue 188 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI1 84) chain D residue 70 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 85) chain D residue 95 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 86) chain D residue 153 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 87) chain D residue 188 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI1 88) chain C residue 275 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 89) chain B residue 88-95 type prosite sequence YVHGSQGC description NITROGENASE_1_1 Nitrogenases component 1 alpha and beta subunits signature 1. YVHGSQGC source prosite : PS00699 90) chain A residue 81-88 type prosite sequence ISHGPVGC description NITROGENASE_1_1 Nitrogenases component 1 alpha and beta subunits signature 1. YVHGSQGC source prosite : PS00699 91) chain B residue 151-165 type prosite sequence TTCMAEVIGDDLNAF description NITROGENASE_1_2 Nitrogenases component 1 alpha and beta subunits signature 2. TTCmaeviGDDLnAF source prosite : PS00090 92) chain A residue 152-166 type prosite sequence SECPIGLIGDDIESV description NITROGENASE_1_2 Nitrogenases component 1 alpha and beta subunits signature 2. TTCmaeviGDDLnAF source prosite : PS00090

Display surface Download Links