9V2L
Complex structure of 2014-422 spike RBD bound to human DPP4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0001618 | molecular_function | virus receptor activity |
| B | 0001666 | biological_process | response to hypoxia |
| B | 0002020 | molecular_function | protease binding |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0005102 | molecular_function | signaling receptor binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005765 | cellular_component | lysosomal membrane |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005925 | cellular_component | focal adhesion |
| B | 0006508 | biological_process | proteolysis |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| B | 0008240 | molecular_function | tripeptidyl-peptidase activity |
| B | 0008284 | biological_process | positive regulation of cell population proliferation |
| B | 0009986 | cellular_component | cell surface |
| B | 0010716 | biological_process | negative regulation of extracellular matrix disassembly |
| B | 0016020 | cellular_component | membrane |
| B | 0016324 | cellular_component | apical plasma membrane |
| B | 0016486 | biological_process | peptide hormone processing |
| B | 0019065 | biological_process | receptor-mediated endocytosis of virus by host cell |
| B | 0030027 | cellular_component | lamellipodium |
| B | 0030139 | cellular_component | endocytic vesicle |
| B | 0031258 | cellular_component | lamellipodium membrane |
| B | 0031295 | biological_process | T cell costimulation |
| B | 0033632 | biological_process | regulation of cell-cell adhesion mediated by integrin |
| B | 0042110 | biological_process | T cell activation |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043542 | biological_process | endothelial cell migration |
| B | 0045121 | cellular_component | membrane raft |
| B | 0045499 | molecular_function | chemorepellent activity |
| B | 0046581 | cellular_component | intercellular canaliculus |
| B | 0046718 | biological_process | symbiont entry into host cell |
| B | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
| B | 0050919 | biological_process | negative chemotaxis |
| B | 0061025 | biological_process | membrane fusion |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070161 | cellular_component | anchoring junction |
| B | 0090024 | biological_process | negative regulation of neutrophil chemotaxis |
| B | 0120116 | biological_process | glucagon processing |
| C | 0001618 | molecular_function | virus receptor activity |
| C | 0001666 | biological_process | response to hypoxia |
| C | 0002020 | molecular_function | protease binding |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0005102 | molecular_function | signaling receptor binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005765 | cellular_component | lysosomal membrane |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0005925 | cellular_component | focal adhesion |
| C | 0006508 | biological_process | proteolysis |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| C | 0008240 | molecular_function | tripeptidyl-peptidase activity |
| C | 0008284 | biological_process | positive regulation of cell population proliferation |
| C | 0009986 | cellular_component | cell surface |
| C | 0010716 | biological_process | negative regulation of extracellular matrix disassembly |
| C | 0016020 | cellular_component | membrane |
| C | 0016324 | cellular_component | apical plasma membrane |
| C | 0016486 | biological_process | peptide hormone processing |
| C | 0019065 | biological_process | receptor-mediated endocytosis of virus by host cell |
| C | 0030027 | cellular_component | lamellipodium |
| C | 0030139 | cellular_component | endocytic vesicle |
| C | 0031258 | cellular_component | lamellipodium membrane |
| C | 0031295 | biological_process | T cell costimulation |
| C | 0033632 | biological_process | regulation of cell-cell adhesion mediated by integrin |
| C | 0042110 | biological_process | T cell activation |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0043542 | biological_process | endothelial cell migration |
| C | 0045121 | cellular_component | membrane raft |
| C | 0045499 | molecular_function | chemorepellent activity |
| C | 0046581 | cellular_component | intercellular canaliculus |
| C | 0046718 | biological_process | symbiont entry into host cell |
| C | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
| C | 0050919 | biological_process | negative chemotaxis |
| C | 0061025 | biological_process | membrane fusion |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 0070161 | cellular_component | anchoring junction |
| C | 0090024 | biological_process | negative regulation of neutrophil chemotaxis |
| C | 0120116 | biological_process | glucagon processing |
Functional Information from PROSITE/UniProt
| site_id | PS00708 |
| Number of Residues | 31 |
| Details | PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV |
| Chain | Residue | Details |
| B | ASP605-VAL635 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 169 |
| Chain | Residue | Details |
| B | TYR547 | electrostatic stabiliser, hydrogen bond donor |
| B | SER630 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | TYR631 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP708 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | HIS740 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 169 |
| Chain | Residue | Details |
| C | TYR547 | electrostatic stabiliser, hydrogen bond donor |
| C | SER630 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | TYR631 | electrostatic stabiliser, hydrogen bond donor |
| C | ASP708 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| C | HIS740 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
