eF-site ID 6cs2-B PDB Code 6cs2 Chain B click to enlarge Title SARS Spike Glycoprotein - human ACE2 complex, Stabilized variant, all ACE2-bound particles Classification viral protein/hydrolase Compound Spike glycoprotein,Fibritin Source (ACE2_HUMAN) Sequence B:  RCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQD LFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNV VRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPF FAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSG NFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLK PIFKLPLGINITNFRAILTAFSPIWGTSAAAYFVGYLKPT TFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIY QTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAW ERKKISNCVADYSVLYNSTFFSTFKCYATKLNDLCFSNVY ADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAW NTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPD GKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFET VCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQ QFGRDVSDFTDSVRDPKTSEILDISPCAFGGVSVITPGTN ASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVF QTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVQKSIVA YTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKT SVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQ DRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTK RSFIEDLLFNKVTQYGECLLICAQKFNGLTVLPPLLTDDM IAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGI GVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQ DVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDPPEA EVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKM SECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVP SQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNF FSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPEL Description (1)  Spike glycoprotein,Envelope glycoprotein, Angiotensin-converting enzyme 2 (E.C.3.4.17.23) Functional site 1) chain B residue 797 type ACT_SITE sequence R description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 29 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 3) chain B residue 65 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 4) chain B residue 73 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 5) chain B residue 109 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 6) chain B residue 118 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 7) chain B residue 119 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 8) chain B residue 158 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 227 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 10) chain B residue 269 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 11) chain B residue 318 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 12) chain B residue 330 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 13) chain B residue 357 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 589 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 602 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 691 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 699 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 783 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 1056 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 1080 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 1116 type ACT_SITE sequence N description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2

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