2RIP
Structure of DPPIV in complex with an inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001618 | molecular_function | virus receptor activity |
| A | 0001662 | biological_process | behavioral fear response |
| A | 0001666 | biological_process | response to hypoxia |
| A | 0002020 | molecular_function | protease binding |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0005102 | molecular_function | signaling receptor binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005765 | cellular_component | lysosomal membrane |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005925 | cellular_component | focal adhesion |
| A | 0006508 | biological_process | proteolysis |
| A | 0007155 | biological_process | cell adhesion |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| A | 0008284 | biological_process | positive regulation of cell population proliferation |
| A | 0009986 | cellular_component | cell surface |
| A | 0010716 | biological_process | negative regulation of extracellular matrix disassembly |
| A | 0016020 | cellular_component | membrane |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0016486 | biological_process | peptide hormone processing |
| A | 0019065 | biological_process | receptor-mediated endocytosis of virus by host cell |
| A | 0030027 | cellular_component | lamellipodium |
| A | 0030139 | cellular_component | endocytic vesicle |
| A | 0031258 | cellular_component | lamellipodium membrane |
| A | 0031295 | biological_process | T cell costimulation |
| A | 0033632 | biological_process | regulation of cell-cell adhesion mediated by integrin |
| A | 0035641 | biological_process | locomotory exploration behavior |
| A | 0036343 | biological_process | psychomotor behavior |
| A | 0042110 | biological_process | T cell activation |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042995 | cellular_component | cell projection |
| A | 0043542 | biological_process | endothelial cell migration |
| A | 0045121 | cellular_component | membrane raft |
| A | 0045499 | molecular_function | chemorepellent activity |
| A | 0046581 | cellular_component | intercellular canaliculus |
| A | 0046718 | biological_process | symbiont entry into host cell |
| A | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
| A | 0050919 | biological_process | negative chemotaxis |
| A | 0061025 | biological_process | membrane fusion |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070161 | cellular_component | anchoring junction |
| A | 0090024 | biological_process | negative regulation of neutrophil chemotaxis |
| A | 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 |
| A | ASP605-VAL635 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084 |
| Chain | Residue | Details |
| A | SER630 | |
| A | ASP708 | |
| A | HIS740 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 |
| Chain | Residue | Details |
| A | ASN85 | |
| A | ASN229 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 |
| Chain | Residue | Details |
| A | ASN92 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 |
| Chain | Residue | Details |
| A | ASN150 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 |
| Chain | Residue | Details |
| A | ASN219 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 |
| Chain | Residue | Details |
| A | ASN281 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 |
| Chain | Residue | Details |
| A | ASN321 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72 |
| Chain | Residue | Details |
| A | ASN520 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218 |
| Chain | Residue | Details |
| A | ASN685 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1jkm |
| Chain | Residue | Details |
| A | HIS740 | |
| A | ASP708 | |
| A | SER630 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1jkm |
| Chain | Residue | Details |
| A | HIS740 | |
| A | SER630 | |
| A | ASP709 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 169 |
| Chain | Residue | Details |
| A | TYR547 | electrostatic stabiliser, hydrogen bond donor |
| A | SER630 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | TYR631 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP708 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS740 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
