8XNF
Cryo-EM structure of SARS-CoV-2 Omicron BA.2.86 spike protein(6P) in complex with human ACE2
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ |
Chain | Residue | Details |
A | THR371-GLN380 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | SITE: Cleavage; by host furin => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32362314, ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616 |
Chain | Residue | Details |
B | GLN689 | |
C | GLN689 | |
D | GLN689 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | SITE: Cleavage; by host TMPRSS2 or CTSL => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616 |
Chain | Residue | Details |
B | ASP819 | |
C | ASP819 | |
D | ASP819 |
site_id | SWS_FT_FI3 |
Number of Residues | 15 |
Details | CARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
Chain | Residue | Details |
B | ASN62 | |
C | PRO1078 | |
D | ASN62 | |
D | THR124 | |
D | VAL721 | |
D | LEU805 | |
D | PRO1078 | |
B | THR124 | |
B | VAL721 | |
B | LEU805 | |
B | PRO1078 | |
C | ASN62 | |
C | THR124 | |
C | VAL721 | |
C | LEU805 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
Chain | Residue | Details |
B | THR76 | |
B | TRP152 | |
C | THR76 | |
C | TRP152 | |
D | THR76 | |
D | TRP152 |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
Chain | Residue | Details |
B | PHE168 | |
C | LEU335 | |
C | PHE347 | |
C | SER620 | |
C | CYS661 | |
C | PHE1102 | |
D | PHE168 | |
D | THR286 | |
D | LEU335 | |
D | PHE347 | |
D | SER620 | |
B | THR286 | |
D | CYS661 | |
D | PHE1102 | |
B | LEU335 | |
B | PHE347 | |
B | SER620 | |
B | CYS661 | |
B | PHE1102 | |
C | PHE168 | |
C | THR286 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
Chain | Residue | Details |
B | PHE238 | |
B | ILE713 | |
C | PHE238 | |
C | ILE713 | |
D | PHE238 | |
D | ILE713 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | CARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391 |
Chain | Residue | Details |
B | VAL327 | |
C | VAL327 | |
D | VAL327 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391 |
Chain | Residue | Details |
B | PHE329 | |
C | PHE329 | |
D | PHE329 |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
Chain | Residue | Details |
B | VAL607 | |
C | VAL607 | |
D | VAL607 |
site_id | SWS_FT_FI10 |
Number of Residues | 6 |
Details | CARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583 |
Chain | Residue | Details |
B | ARG680 | |
B | SER682 | |
C | ARG680 | |
C | SER682 | |
D | ARG680 | |
D | SER682 |
site_id | SWS_FT_FI11 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
Chain | Residue | Details |
B | ASP1138 | |
C | ASP1138 | |
D | ASP1138 |