eF-site ID 2nyy-ACD PDB Code 2nyy Chain A, C, D click to enlarge Title Crystal structure of botulinum neurotoxin type A complexed with monoclonal antibody CR1 Classification TOXIN/IMMUNE SYSTEM Compound Botulinum neurotoxin type A Source ORGANISM_SCIENTIFIC: Clostridium botulinum; Sequence A:  PFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNK IWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTD NEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGS TIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADII QFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLE VDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNR VFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENE FRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKY LLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVL NRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANF NGQNTEINNMNFTKLKNFTGLFEFYKLLCVRLCIKVNNWD LFFSPSEDNFTNDLNKGEEITSDTNIEANISLDLIQQYYL TFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKYE LDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYT FFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVSIA DITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFI PEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDE VYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIIN YQYNQYTEEEKNNINFNIDDLSSKLNESINKAMININKFL NQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRG TLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLLSTFTE YIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDP IDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIR IPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQ DTQEIKQRVVFKYSQMINISDYINRWIFVTITNNRLNNSK IYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIW IKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGDYLQYD KPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNI YLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKN KEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKND QGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVASNWYN RQIERSSRTLGCSWEFIPVDDGWGERP C:  EIVLTQSPATLSLSPGERATISCRASESVDSYGHSFMQWY QQKPGQAPRLLIYRASNLEPGIPARFSGSGSGTDFTLTIS SLEPEDFAVYYCQQGNEVPFTFGQGTKVEIKRTVAAPSVF IFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQS GNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEV THQGLSSPVTKSFNRG D:  VQLQESGGGLVQPGGSLRLSCAASGFTFKYDYMYWVRQAP GKGLEWVATISDGGSYTYYSDSVEGRFTTSRDNSKNTLYL QMNSLRAEDTAIYYCSRYRYDDAMDYWGQGTLVTVSSAST KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNS GALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYIC NVNHKPSNTKVDKKVEP Description Functional site 1) chain A residue 223 type sequence H description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 2) chain A residue 227 type sequence H description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 3) chain A residue 262 type sequence E description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 4) chain A residue 279 type sequence E description BINDING SITE FOR RESIDUE CA A 1297 source : AC2 5) chain A residue 347 type sequence E description BINDING SITE FOR RESIDUE CA A 1297 source : AC2 6) chain A residue 220-229 type prosite sequence TLAHELIHAG description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLAHELIHAG source prosite : PS00142 7) chain C residue 196-202 type prosite sequence YACEVTH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH source prosite : PS00290 8) chain D residue 199-205 type prosite sequence YICNVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH source prosite : PS00290 9) chain A residue 628-648 type TRANSMEM sequence ADITIIIPYIGPALNIGNMLY description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 657-677 type TRANSMEM sequence IFSGAVILLEFIPEIAIPVLG description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 225 type ACT_SITE sequence L description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 224 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:17173035, ECO:0000305|PubMed:9783750, ECO:0007744|PDB:2NYY, ECO:0007744|PDB:2NZ9, ECO:0007744|PDB:3BTA, ECO:0007744|PDB:3QIX, ECO:0007744|PDB:3QIY, ECO:0007744|PDB:3QIZ, ECO:0007744|PDB:3QJ0 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 228 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:17173035, ECO:0000305|PubMed:9783750, ECO:0007744|PDB:2NYY, ECO:0007744|PDB:2NZ9, ECO:0007744|PDB:3BTA, ECO:0007744|PDB:3QIX, ECO:0007744|PDB:3QIY, ECO:0007744|PDB:3QIZ, ECO:0007744|PDB:3QJ0 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 263 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:17173035, ECO:0007744|PDB:2NYY, ECO:0007744|PDB:2NZ9, ECO:0007744|PDB:3BTA, ECO:0007744|PDB:3QIX, ECO:0007744|PDB:3QIY, ECO:0007744|PDB:3QIZ, ECO:0007744|PDB:3QJ0 source Swiss-Prot : SWS_FT_FI4 15) chain A residue 1118 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18704164, ECO:0000269|PubMed:27958736, ECO:0007744|PDB:2VU9, ECO:0007744|PDB:5TPB, ECO:0007744|PDB:5TPC source Swiss-Prot : SWS_FT_FI5 16) chain A residue 1204 type BINDING sequence K description BINDING => ECO:0000269|PubMed:18704164, ECO:0000269|PubMed:27958736, ECO:0000305|PubMed:14731268, ECO:0007744|PDB:2VU9, ECO:0007744|PDB:5TPB, ECO:0007744|PDB:5TPC source Swiss-Prot : SWS_FT_FI6 17) chain A residue 364 type SITE sequence K description Transition state stabilizer => ECO:0000305|PubMed:11827515 source Swiss-Prot : SWS_FT_FI7 18) chain A residue 367 type SITE sequence L description Transition state stabilizer => ECO:0000305|PubMed:11827515 source Swiss-Prot : SWS_FT_FI7

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