8I9D
S-ECD (Omicron XBB.1) in complex with PD of 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 |
F | THR371-GLN380 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402 |
Chain | Residue | Details |
F | GLU375 | |
D | GLU375 | |
E | GLU375 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
F | HIS505 | |
D | HIS505 | |
E | HIS505 |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774 |
Chain | Residue | Details |
F | ARG169 | |
F | TRP477 | |
F | LYS481 | |
D | ARG169 | |
D | TRP477 | |
D | LYS481 | |
E | ARG169 | |
E | TRP477 | |
E | LYS481 |
site_id | SWS_FT_FI4 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
F | ARG273 | |
F | HIS345 | |
F | TYR515 | |
D | ARG273 | |
D | HIS345 | |
D | TYR515 | |
E | ARG273 | |
E | HIS345 | |
E | TYR515 | |
B | ALA1078 | |
C | TRP64 | |
C | ASN125 | |
C | SER721 | |
C | ILE805 | |
C | ALA1078 |
site_id | SWS_FT_FI5 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
F | HIS374 | |
F | HIS378 | |
F | GLU402 | |
D | HIS374 | |
D | HIS378 | |
D | GLU402 | |
E | HIS374 | |
E | HIS378 | |
E | GLU402 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
F | ASN53 | |
F | ASN322 | |
D | ASN53 | |
D | ASN322 | |
E | ASN53 | |
E | ASN322 | |
A | TRP1102 | |
B | GLU169 | |
B | THR286 | |
B | LEU335 | |
B | PHE347 | |
B | VAL620 | |
B | GLU661 | |
B | TRP1102 | |
C | GLU169 | |
C | THR286 | |
C | LEU335 | |
C | PHE347 | |
C | VAL620 | |
C | GLU661 | |
C | TRP1102 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337 |
Chain | Residue | Details |
F | ASN90 | |
D | ASN90 | |
E | ASN90 | |
B | ALA713 | |
C | PHE238 | |
C | ALA713 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
F | ASN103 | |
F | ASN432 | |
D | ASN103 | |
D | ASN432 | |
E | ASN103 | |
E | ASN432 |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337 |
Chain | Residue | Details |
F | ASN546 | |
D | ASN546 | |
E | ASN546 |
site_id | SWS_FT_FI10 |
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 |
A | GLN607 | |
B | GLN607 | |
C | GLN607 |
site_id | SWS_FT_FI11 |
Number of Residues | 6 |
Details | CARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583 |
Chain | Residue | Details |
A | SER680 | |
A | GLY682 | |
B | SER680 | |
B | GLY682 | |
C | SER680 | |
C | GLY682 |
site_id | SWS_FT_FI12 |
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 |
A | TYR1138 | |
B | TYR1138 | |
C | TYR1138 |