eF-site ID 7kj4-D PDB Code 7kj4 Chain D click to enlarge Title SARS-CoV-2 Spike Glycoprotein with three ACE2 Bound Classification VIRAL PROTEIN/HYDROLASE Compound Spike glycoprotein Source (ACE2_HUMAN) Sequence D:  IEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQ NMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQAL QQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQE CLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLY EEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRG QLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIG CLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQ AWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQ KAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQ YDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKS IGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWR WMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDP ASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLH KCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMN VRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPY Description (1)  Spike glycoprotein Functional site 1) chain D residue 371-380 type prosite sequence TAHHEMGHIQ description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ source prosite : PS00142 2) chain D residue 169 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774 source Swiss-Prot : SWS_FT_FI3 3) chain D residue 477 type BINDING sequence W description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774 source Swiss-Prot : SWS_FT_FI3 4) chain D residue 481 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774 source Swiss-Prot : SWS_FT_FI3 5) chain D residue 53 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI6 6) chain D residue 322 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI6 7) chain D residue 273 type BINDING sequence R description BINDING => ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI4 8) chain D residue 345 type BINDING sequence H description BINDING => ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI4 9) chain D residue 515 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI4 10) chain D residue 374 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 source Swiss-Prot : SWS_FT_FI5 11) chain D residue 378 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 source Swiss-Prot : SWS_FT_FI5 12) chain D residue 402 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 source Swiss-Prot : SWS_FT_FI5 13) chain D residue 90 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337 source Swiss-Prot : SWS_FT_FI7 14) chain D residue 546 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337 source Swiss-Prot : SWS_FT_FI9 15) chain D residue 375 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402 source Swiss-Prot : SWS_FT_FI1 16) chain D residue 505 type ACT_SITE sequence H description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 source Swiss-Prot : SWS_FT_FI2 17) chain D residue 103 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 source Swiss-Prot : SWS_FT_FI8 18) chain D residue 432 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 source Swiss-Prot : SWS_FT_FI8

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