7UFL
Crystal structure of chimeric omicron RBD (strain BA.2) complexed with chimeric mouse ACE2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| A | 0016020 | cellular_component | membrane |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| B | 0016020 | cellular_component | membrane |
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 |
| E | SER323 | |
| F | SER323 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391 |
| Chain | Residue | Details |
| E | ASP325 | |
| F | ASP325 |
| 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 |
| E | ASN331 | |
| E | ASN343 | |
| F | ASN331 | |
| F | ASN343 | |
| B | TRP477 | |
| B | LYS481 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| A | ARG273 | |
| A | HIS345 | |
| A | TYR515 | |
| B | ARG273 | |
| B | HIS345 | |
| B | TYR515 |
| site_id | SWS_FT_FI5 |
| 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 | |
| B | HIS374 | |
| B | HIS378 | |
| B | GLU402 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| A | ASN53 | |
| A | HIS322 | |
| B | ASN53 | |
| B | HIS322 |
| site_id | SWS_FT_FI7 |
| 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 | THR90 | |
| B | THR90 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
| Chain | Residue | Details |
| A | ASN103 | |
| A | ASN432 | |
| B | ASN103 | |
| B | ASN432 |
| site_id | SWS_FT_FI9 |
| 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 | |
| B | ASN546 |
