eF-site ID 1n6e-ABCDEFGHIJKL PDB Code 1n6e Chain A, B, C, D, E, F, G, H, I, J, K, L Title tricorn protease in complex with a tridecapeptide chloromethyl ketone derivative Classification HYDROLASE Compound Tricorn protease Source Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) (1N6E) Sequence A:  MPNLLLNPDIHGDRIIFVCCDDLWEHDLKSGSTRKIVSNL GVINNARFFPDGRKIAIRVMRGSSLNTADLYFYNGENGEI KRITYFSGKSTGRRMFTDVAGFDPDGNLIISTDAMQPFSS MTCLYRVENDGINFVPLNLGPATHILFADGRRVIGRNTFE LPHWKGYRGGTRGKIWIEVNSGAFKKIVDMSTHVSSPVIV GHRIYFITDIDGFGQIYSTDLDGKDLRKHTSFTDYYPRHL NTDGRRILFSKGGSIYIFNPDTEKIEKIEIGDLESPEDRI ISIPSKFAEDFSPLDGDLIAFVSRGQAFIQDVSGTYVLKV PEPLRIRYVRRGGDTKVAFIHGTREGDFLGIYDYRTGKAE KFEENLGNVFAMGVDRNGKFAVVANDRFEIMTVDLETGKP TVIERSREAMITDFTISDNSRFIAYGFPLKHGETDGYVMQ AIHVYDMEGRKIFAATTENSHDYAPAFDADSKNLYYLSYR SLDPSPDRVVLNFSFEVVSKPFVIPLIPGSPNPTKLVPRS MTSEAGEYDLNDMYKRSSPINVDPGDYRMIIPLESSILIY SVPVHGEFAAYYQGAPEKGVLLKYDVKTRKVTEVKNNLTD LRLSADRKTVMVRKDDGKIYTFPLEKPEDERTVETDKRPL VSSIHEEFLQMYDEAWKLARDNYWNEAVAKEISERIYEKY RNLVPLCKTRYDLSNVIVEMQGEYRTSHSYEMGGTFTDKD PFRSGRIACDFKLDGDHYVVAKAYAGDYSNEGEKSPIFEY GIDPTGYLIEDIDGETVGAGSNIYRVLSEKAGTSARIRLS GKGGDKRDLMIDILDDDRFIRYRSWVEANRRYVHERSKGT IGYIHIPDMGMMGLNEFYRLFINESSYQGLIVDVRFNGGG FVSQLIIEKLMNKRIGYDNPRRGTLSPYPTNSVRGKIIAI TNEYAGSDGDIFSFSFKKLGLGKLIGTRTWGGVVGITPKR RLIDGTVLTQPEFAFWFRDAGFGVENYGVDPDVEIEYAPH DYLSGKDPQIDYAIDALIEELRN B:  TQKAAAELTFFX C:  MPNLLLNPDIHGDRIIFVCCDDLWEHDLKSGSTRKIVSNL GVINNARFFPDGRKIAIRVMRGSSLNTADLYFYNGENGEI KRITYFSGKSTGRRMFTDVAGFDPDGNLIISTDAMQPFSS MTCLYRVENDGINFVPLNLGPATHILFADGRRVIGRNTFE LPHWKGYRGGTRGKIWIEVNSGAFKKIVDMSTHVSSPVIV GHRIYFITDIDGFGQIYSTDLDGKDLRKHTSFTDYYPRHL NTDGRRILFSKGGSIYIFNPDTEKIEKIEIGDLESPEDRI ISIPSKFAEDFSPLDGDLIAFVSRGQAFIQDVSGTYVLKV PEPLRIRYVRRGGDTKVAFIHGTREGDFLGIYDYRTGKAE KFEENLGNVFAMGVDRNGKFAVVANDRFEIMTVDLETGKP TVIERSREAMITDFTISDNSRFIAYGFPLKHGETDGYVMQ AIHVYDMEGRKIFAATTENSHDYAPAFDADSKNLYYLSYR SLDPSPDRVVLNFSFEVVSKPFVIPLIPGSPNPTKLVPRS MTSEAGEYDLNDMYKRSSPINVDPGDYRMIIPLESSILIY SVPVHGEFAAYYQGAPEKGVLLKYDVKTRKVTEVKNNLTD LRLSADRKTVMVRKDDGKIYTFPLEKPEDERTVETDKRPL VSSIHEEFLQMYDEAWKLARDNYWNEAVAKEISERIYEKY RNLVPLCKTRYDLSNVIVEMQGEYRTSHSYEMGGTFTDKD PFRSGRIACDFKLDGDHYVVAKAYAGDYSNEGEKSPIFEY GIDPTGYLIEDIDGETVGAGSNIYRVLSEKAGTSARIRLS GKGGDKRDLMIDILDDDRFIRYRSWVEANRRYVHERSKGT IGYIHIPDMGMMGLNEFYRLFINESSYQGLIVDVRFNGGG FVSQLIIEKLMNKRIGYDNPRRGTLSPYPTNSVRGKIIAI TNEYAGSDGDIFSFSFKKLGLGKLIGTRTWGGVVGITPKR RLIDGTVLTQPEFAFWFRDAGFGVENYGVDPDVEIEYAPH DYLSGKDPQIDYAIDALIEELRN D:  TQKAAAELTFFX E:  MPNLLLNPDIHGDRIIFVCCDDLWEHDLKSGSTRKIVSNL GVINNARFFPDGRKIAIRVMRGSSLNTADLYFYNGENGEI KRITYFSGKSTGRRMFTDVAGFDPDGNLIISTDAMQPFSS MTCLYRVENDGINFVPLNLGPATHILFADGRRVIGRNTFE LPHWKGYRGGTRGKIWIEVNSGAFKKIVDMSTHVSSPVIV GHRIYFITDIDGFGQIYSTDLDGKDLRKHTSFTDYYPRHL NTDGRRILFSKGGSIYIFNPDTEKIEKIEIGDLESPEDRI ISIPSKFAEDFSPLDGDLIAFVSRGQAFIQDVSGTYVLKV PEPLRIRYVRRGGDTKVAFIHGTREGDFLGIYDYRTGKAE KFEENLGNVFAMGVDRNGKFAVVANDRFEIMTVDLETGKP TVIERSREAMITDFTISDNSRFIAYGFPLKHGETDGYVMQ AIHVYDMEGRKIFAATTENSHDYAPAFDADSKNLYYLSYR SLDPSPDRVVLNFSFEVVSKPFVIPLIPGSPNPTKLVPRS MTSEAGEYDLNDMYKRSSPINVDPGDYRMIIPLESSILIY SVPVHGEFAAYYQGAPEKGVLLKYDVKTRKVTEVKNNLTD LRLSADRKTVMVRKDDGKIYTFPLEKPEDERTVETDKRPL VSSIHEEFLQMYDEAWKLARDNYWNEAVAKEISERIYEKY RNLVPLCKTRYDLSNVIVEMQGEYRTSHSYEMGGTFTDKD PFRSGRIACDFKLDGDHYVVAKAYAGDYSNEGEKSPIFEY GIDPTGYLIEDIDGETVGAGSNIYRVLSEKAGTSARIRLS GKGGDKRDLMIDILDDDRFIRYRSWVEANRRYVHERSKGT IGYIHIPDMGMMGLNEFYRLFINESSYQGLIVDVRFNGGG FVSQLIIEKLMNKRIGYDNPRRGTLSPYPTNSVRGKIIAI TNEYAGSDGDIFSFSFKKLGLGKLIGTRTWGGVVGITPKR RLIDGTVLTQPEFAFWFRDAGFGVENYGVDPDVEIEYAPH DYLSGKDPQIDYAIDALIEELRN F:  TQKAAAELTFFX G:  MPNLLLNPDIHGDRIIFVCCDDLWEHDLKSGSTRKIVSNL GVINNARFFPDGRKIAIRVMRGSSLNTADLYFYNGENGEI KRITYFSGKSTGRRMFTDVAGFDPDGNLIISTDAMQPFSS MTCLYRVENDGINFVPLNLGPATHILFADGRRVIGRNTFE LPHWKGYRGGTRGKIWIEVNSGAFKKIVDMSTHVSSPVIV GHRIYFITDIDGFGQIYSTDLDGKDLRKHTSFTDYYPRHL NTDGRRILFSKGGSIYIFNPDTEKIEKIEIGDLESPEDRI ISIPSKFAEDFSPLDGDLIAFVSRGQAFIQDVSGTYVLKV PEPLRIRYVRRGGDTKVAFIHGTREGDFLGIYDYRTGKAE KFEENLGNVFAMGVDRNGKFAVVANDRFEIMTVDLETGKP TVIERSREAMITDFTISDNSRFIAYGFPLKHGETDGYVMQ AIHVYDMEGRKIFAATTENSHDYAPAFDADSKNLYYLSYR SLDPSPDRVVLNFSFEVVSKPFVIPLIPGSPNPTKLVPRS MTSEAGEYDLNDMYKRSSPINVDPGDYRMIIPLESSILIY SVPVHGEFAAYYQGAPEKGVLLKYDVKTRKVTEVKNNLTD LRLSADRKTVMVRKDDGKIYTFPLEKPEDERTVETDKRPL VSSIHEEFLQMYDEAWKLARDNYWNEAVAKEISERIYEKY RNLVPLCKTRYDLSNVIVEMQGEYRTSHSYEMGGTFTDKD PFRSGRIACDFKLDGDHYVVAKAYAGDYSNEGEKSPIFEY GIDPTGYLIEDIDGETVGAGSNIYRVLSEKAGTSARIRLS GKGGDKRDLMIDILDDDRFIRYRSWVEANRRYVHERSKGT IGYIHIPDMGMMGLNEFYRLFINESSYQGLIVDVRFNGGG FVSQLIIEKLMNKRIGYDNPRRGTLSPYPTNSVRGKIIAI TNEYAGSDGDIFSFSFKKLGLGKLIGTRTWGGVVGITPKR RLIDGTVLTQPEFAFWFRDAGFGVENYGVDPDVEIEYAPH DYLSGKDPQIDYAIDALIEELRN H:  TQKAAAELTFFX I:  MPNLLLNPDIHGDRIIFVCCDDLWEHDLKSGSTRKIVSNL GVINNARFFPDGRKIAIRVMRGSSLNTADLYFYNGENGEI KRITYFSGKSTGRRMFTDVAGFDPDGNLIISTDAMQPFSS MTCLYRVENDGINFVPLNLGPATHILFADGRRVIGRNTFE LPHWKGYRGGTRGKIWIEVNSGAFKKIVDMSTHVSSPVIV GHRIYFITDIDGFGQIYSTDLDGKDLRKHTSFTDYYPRHL NTDGRRILFSKGGSIYIFNPDTEKIEKIEIGDLESPEDRI ISIPSKFAEDFSPLDGDLIAFVSRGQAFIQDVSGTYVLKV PEPLRIRYVRRGGDTKVAFIHGTREGDFLGIYDYRTGKAE KFEENLGNVFAMGVDRNGKFAVVANDRFEIMTVDLETGKP TVIERSREAMITDFTISDNSRFIAYGFPLKHGETDGYVMQ AIHVYDMEGRKIFAATTENSHDYAPAFDADSKNLYYLSYR SLDPSPDRVVLNFSFEVVSKPFVIPLIPGSPNPTKLVPRS MTSEAGEYDLNDMYKRSSPINVDPGDYRMIIPLESSILIY SVPVHGEFAAYYQGAPEKGVLLKYDVKTRKVTEVKNNLTD LRLSADRKTVMVRKDDGKIYTFPLEKPEDERTVETDKRPL VSSIHEEFLQMYDEAWKLARDNYWNEAVAKEISERIYEKY RNLVPLCKTRYDLSNVIVEMQGEYRTSHSYEMGGTFTDKD PFRSGRIACDFKLDGDHYVVAKAYAGDYSNEGEKSPIFEY GIDPTGYLIEDIDGETVGAGSNIYRVLSEKAGTSARIRLS GKGGDKRDLMIDILDDDRFIRYRSWVEANRRYVHERSKGT IGYIHIPDMGMMGLNEFYRLFINESSYQGLIVDVRFNGGG FVSQLIIEKLMNKRIGYDNPRRGTLSPYPTNSVRGKIIAI TNEYAGSDGDIFSFSFKKLGLGKLIGTRTWGGVVGITPKR RLIDGTVLTQPEFAFWFRDAGFGVENYGVDPDVEIEYAPH DYLSGKDPQIDYAIDALIEELRN J:  TQKAAAELTFFX K:  MPNLLLNPDIHGDRIIFVCCDDLWEHDLKSGSTRKIVSNL GVINNARFFPDGRKIAIRVMRGSSLNTADLYFYNGENGEI KRITYFSGKSTGRRMFTDVAGFDPDGNLIISTDAMQPFSS MTCLYRVENDGINFVPLNLGPATHILFADGRRVIGRNTFE LPHWKGYRGGTRGKIWIEVNSGAFKKIVDMSTHVSSPVIV GHRIYFITDIDGFGQIYSTDLDGKDLRKHTSFTDYYPRHL NTDGRRILFSKGGSIYIFNPDTEKIEKIEIGDLESPEDRI ISIPSKFAEDFSPLDGDLIAFVSRGQAFIQDVSGTYVLKV PEPLRIRYVRRGGDTKVAFIHGTREGDFLGIYDYRTGKAE KFEENLGNVFAMGVDRNGKFAVVANDRFEIMTVDLETGKP TVIERSREAMITDFTISDNSRFIAYGFPLKHGETDGYVMQ AIHVYDMEGRKIFAATTENSHDYAPAFDADSKNLYYLSYR SLDPSPDRVVLNFSFEVVSKPFVIPLIPGSPNPTKLVPRS MTSEAGEYDLNDMYKRSSPINVDPGDYRMIIPLESSILIY SVPVHGEFAAYYQGAPEKGVLLKYDVKTRKVTEVKNNLTD LRLSADRKTVMVRKDDGKIYTFPLEKPEDERTVETDKRPL VSSIHEEFLQMYDEAWKLARDNYWNEAVAKEISERIYEKY RNLVPLCKTRYDLSNVIVEMQGEYRTSHSYEMGGTFTDKD PFRSGRIACDFKLDGDHYVVAKAYAGDYSNEGEKSPIFEY GIDPTGYLIEDIDGETVGAGSNIYRVLSEKAGTSARIRLS GKGGDKRDLMIDILDDDRFIRYRSWVEANRRYVHERSKGT IGYIHIPDMGMMGLNEFYRLFINESSYQGLIVDVRFNGGG FVSQLIIEKLMNKRIGYDNPRRGTLSPYPTNSVRGKIIAI TNEYAGSDGDIFSFSFKKLGLGKLIGTRTWGGVVGITPKR RLIDGTVLTQPEFAFWFRDAGFGVENYGVDPDVEIEYAPH DYLSGKDPQIDYAIDALIEELRN L:  TQKAAAELTFFX Description Functional site 1) chain A residue 746 type sequence H description BINDING SITE FOR RESIDUE 0QE B 1214 source : AC1 2) chain A residue 965 type sequence S description BINDING SITE FOR RESIDUE 0QE B 1214 source : AC1 3) chain A residue 966 type sequence D description BINDING SITE FOR RESIDUE 0QE B 1214 source : AC1 4) chain B residue 1213 type sequence F description BINDING SITE FOR RESIDUE 0QE B 1214 source : AC1 5) chain C residue 746 type sequence H description BINDING SITE FOR RESIDUE 0QE D 1214 source : AC2 6) chain C residue 965 type sequence S description BINDING SITE FOR RESIDUE 0QE D 1214 source : AC2 7) chain C residue 966 type sequence D description BINDING SITE FOR RESIDUE 0QE D 1214 source : AC2 8) chain D residue 1213 type sequence F description BINDING SITE FOR RESIDUE 0QE D 1214 source : AC2 9) chain E residue 746 type sequence H description BINDING SITE FOR RESIDUE 0QE F 1214 source : AC3 10) chain E residue 965 type sequence S description BINDING SITE FOR RESIDUE 0QE F 1214 source : AC3 11) chain E residue 966 type sequence D description BINDING SITE FOR RESIDUE 0QE F 1214 source : AC3 12) chain F residue 1213 type sequence F description BINDING SITE FOR RESIDUE 0QE F 1214 source : AC3 13) chain G residue 746 type sequence H description BINDING SITE FOR RESIDUE 0QE H 1214 source : AC4 14) chain G residue 965 type sequence S description BINDING SITE FOR RESIDUE 0QE H 1214 source : AC4 15) chain G residue 966 type sequence D description BINDING SITE FOR RESIDUE 0QE H 1214 source : AC4 16) chain H residue 1213 type sequence F description BINDING SITE FOR RESIDUE 0QE H 1214 source : AC4 17) chain I residue 746 type sequence H description BINDING SITE FOR RESIDUE 0QE J 1214 source : AC5 18) chain I residue 965 type sequence S description BINDING SITE FOR RESIDUE 0QE J 1214 source : AC5 19) chain I residue 966 type sequence D description BINDING SITE FOR RESIDUE 0QE J 1214 source : AC5 20) chain J residue 1213 type sequence F description BINDING SITE FOR RESIDUE 0QE J 1214 source : AC5 21) chain K residue 746 type sequence H description BINDING SITE FOR RESIDUE 0QE L 1214 source : AC6 22) chain K residue 965 type sequence S description BINDING SITE FOR RESIDUE 0QE L 1214 source : AC6 23) chain K residue 966 type sequence D description BINDING SITE FOR RESIDUE 0QE L 1214 source : AC6 24) chain L residue 1213 type sequence F description BINDING SITE FOR RESIDUE 0QE L 1214 source : AC6 25) chain A residue 746 type catalytic sequence H description 808 source MCSA : MCSA1 26) chain A residue 918 type catalytic sequence G description 808 source MCSA : MCSA1 27) chain A residue 965 type catalytic sequence S description 808 source MCSA : MCSA1 28) chain A residue 966 type catalytic sequence D description 808 source MCSA : MCSA1 29) chain C residue 746 type catalytic sequence H description 808 source MCSA : MCSA2 30) chain C residue 918 type catalytic sequence G description 808 source MCSA : MCSA2 31) chain C residue 965 type catalytic sequence S description 808 source MCSA : MCSA2 32) chain C residue 966 type catalytic sequence D description 808 source MCSA : MCSA2 33) chain E residue 746 type catalytic sequence H description 808 source MCSA : MCSA3 34) chain E residue 918 type catalytic sequence G description 808 source MCSA : MCSA3 35) chain E residue 965 type catalytic sequence S description 808 source MCSA : MCSA3 36) chain E residue 966 type catalytic sequence D description 808 source MCSA : MCSA3 37) chain G residue 746 type catalytic sequence H description 808 source MCSA : MCSA4 38) chain G residue 918 type catalytic sequence G description 808 source MCSA : MCSA4 39) chain G residue 965 type catalytic sequence S description 808 source MCSA : MCSA4 40) chain G residue 966 type catalytic sequence D description 808 source MCSA : MCSA4 41) chain I residue 746 type catalytic sequence H description 808 source MCSA : MCSA5 42) chain I residue 918 type catalytic sequence G description 808 source MCSA : MCSA5 43) chain I residue 965 type catalytic sequence S description 808 source MCSA : MCSA5 44) chain I residue 966 type catalytic sequence D description 808 source MCSA : MCSA5 45) chain K residue 746 type catalytic sequence H description 808 source MCSA : MCSA6 46) chain K residue 918 type catalytic sequence G description 808 source MCSA : MCSA6 47) chain K residue 965 type catalytic sequence S description 808 source MCSA : MCSA6 48) chain K residue 966 type catalytic sequence D description 808 source MCSA : MCSA6 49) chain A residue 916 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI4 50) chain C residue 916 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI4 51) chain E residue 916 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI4 52) chain G residue 916 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI4 53) chain I residue 916 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI4 54) chain K residue 916 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 746 type ACT_SITE sequence H description Charge relay system => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI1 56) chain C residue 746 type ACT_SITE sequence H description Charge relay system => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI1 57) chain E residue 746 type ACT_SITE sequence H description Charge relay system => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI1 58) chain G residue 746 type ACT_SITE sequence H description Charge relay system => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI1 59) chain I residue 746 type ACT_SITE sequence H description Charge relay system => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI1 60) chain K residue 746 type ACT_SITE sequence H description Charge relay system => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI1 61) chain A residue 965 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI2 62) chain C residue 965 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI2 63) chain E residue 965 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI2 64) chain G residue 965 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI2 65) chain I residue 965 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI2 66) chain K residue 965 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI2 67) chain A residue 1023 type ACT_SITE sequence E description Charge relay system => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI3 68) chain C residue 1023 type ACT_SITE sequence E description Charge relay system => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI3 69) chain E residue 1023 type ACT_SITE sequence E description Charge relay system => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI3 70) chain G residue 1023 type ACT_SITE sequence E description Charge relay system => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI3 71) chain I residue 1023 type ACT_SITE sequence E description Charge relay system => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI3 72) chain K residue 1023 type ACT_SITE sequence E description Charge relay system => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI3 73) chain A residue 993 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI5 74) chain C residue 993 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI5 75) chain E residue 993 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI5 76) chain G residue 993 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI5 77) chain I residue 993 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI5 78) chain K residue 993 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI5 79) chain A residue 936 type SITE sequence D description Substrate specificity switch => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI6 80) chain C residue 936 type SITE sequence D description Substrate specificity switch => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI6 81) chain E residue 936 type SITE sequence D description Substrate specificity switch => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI6 82) chain G residue 936 type SITE sequence D description Substrate specificity switch => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI6 83) chain I residue 936 type SITE sequence D description Substrate specificity switch => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI6 84) chain K residue 936 type SITE sequence D description Substrate specificity switch => ECO:0000269|PubMed:11719810 source Swiss-Prot : SWS_FT_FI6 85) chain A residue 966 type SITE sequence D description Transition state stabilizer; via amide nitrogen => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI7 86) chain C residue 966 type SITE sequence D description Transition state stabilizer; via amide nitrogen => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI7 87) chain E residue 966 type SITE sequence D description Transition state stabilizer; via amide nitrogen => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI7 88) chain G residue 966 type SITE sequence D description Transition state stabilizer; via amide nitrogen => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI7 89) chain I residue 966 type SITE sequence D description Transition state stabilizer; via amide nitrogen => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI7 90) chain K residue 966 type SITE sequence D description Transition state stabilizer; via amide nitrogen => ECO:0000269|PubMed:11719810, ECO:0000269|PubMed:12470958 source Swiss-Prot : SWS_FT_FI7

Display surface Download Links