8WDR
Crystal structure of BQ.1.1 RBD complexed 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 | 2 |
Details | CARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391 |
Chain | Residue | Details |
B | THR323 | |
D | THR323 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391 |
Chain | Residue | Details |
B | SER325 | |
D | SER325 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
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 | ASN331 | |
B | ASN343 | |
D | ASN331 | |
D | ASN343 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402 |
Chain | Residue | Details |
A | GLU375 | |
C | GLU375 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
A | HIS505 | |
C | HIS505 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774 |
Chain | Residue | Details |
A | ARG169 | |
A | TRP477 | |
A | LYS481 | |
C | ARG169 | |
C | TRP477 | |
C | LYS481 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
A | ARG273 | |
A | HIS345 | |
A | TYR515 | |
C | ARG273 | |
C | HIS345 | |
C | TYR515 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
A | HIS374 | |
A | HIS378 | |
A | GLU402 | |
C | HIS374 | |
C | HIS378 | |
C | GLU402 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498 |
Chain | Residue | Details |
A | TYR781 | |
C | TYR781 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498 |
Chain | Residue | Details |
A | SER783 | |
C | SER783 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
A | ASN53 | |
A | ASN322 | |
C | ASN53 | |
C | ASN322 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337 |
Chain | Residue | Details |
A | ASN90 | |
C | ASN90 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
A | ASN103 | |
A | ASN432 | |
C | ASN103 | |
C | ASN432 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337 |
Chain | Residue | Details |
A | ASN546 | |
C | ASN546 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN690 | |
C | ASN690 |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36876523 |
Chain | Residue | Details |
A | LYS788 | |
C | LYS788 |