eF-site ID 6cs2-A PDB Code 6cs2 Chain A 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 A:  RCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQD LFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNV VRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPF FAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSG NFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLK PIFKLPLGINITNFRAILTAFSPIWGTSAAAYFVGYLKPT TFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIY QTSNFRVVPSGDVVRFPNLSTDLIKNQCVNFNFNGLTGTG VLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPC AFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLT PAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGI CASYHTVKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISI TTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQ LNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNF SQILPDPLKPTKRSFIEDLLFNKVQYGECLGDLICAQKFN GLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQI PFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQE SLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSV LNDILSRLDPPEAEVQIDRLITGRLQSLQTYVTQQLIRAA EIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAA PHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFV FNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNT VYDPLQPELDS Description (1)  Spike glycoprotein,Envelope glycoprotein, Angiotensin-converting enzyme 2 (E.C.3.4.17.23) Functional site 1) chain A 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 A 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 3) chain A 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 4) chain A 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 5) chain A 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 6) chain A 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 7) chain A 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 8) chain A 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 9) chain A 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 10) chain A 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 11) chain A 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 12) chain A 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 13) chain A 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 14) chain A 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 15) chain A 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 16) chain A 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 17) chain A 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 18) chain A 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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