7XBG
The crystal structure of RshSTT182/200 RBD-insert2-T346R-Y496G mutant in complex with human 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 |
C | 0006508 | biological_process | proteolysis |
C | 0008237 | molecular_function | metallopeptidase activity |
C | 0008241 | molecular_function | peptidyl-dipeptidase activity |
C | 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 | 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_FI2 |
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_FI3 |
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_FI4 |
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_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 | |
C | HIS374 | |
C | HIS378 | |
C | 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 | ASN322 | |
C | ASN53 | |
C | ASN322 |
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 | ASN90 | |
C | ASN90 |
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 | |
C | ASN103 | |
C | 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 | |
C | ASN546 |