3LE7
Crystal structure of PD-L1 from P. dioica in complex with adenine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006952 | biological_process | defense response |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017148 | biological_process | negative regulation of translation |
| A | 0030598 | molecular_function | rRNA N-glycosylase activity |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0090729 | molecular_function | toxin activity |
| B | 0006952 | biological_process | defense response |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017148 | biological_process | negative regulation of translation |
| B | 0030598 | molecular_function | rRNA N-glycosylase activity |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0090729 | molecular_function | toxin activity |
Functional Information from PROSITE/UniProt
| site_id | PS00275 |
| Number of Residues | 17 |
| Details | SHIGA_RICIN Shiga/ricin ribosomal inactivating toxins active site signature. IqMVsEAARFKyIEnqV |
| Chain | Residue | Details |
| A | ILE173-VAL189 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P84531","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20174685","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LE7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in PD-L1 and PD-L2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19014994","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19452522","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20174685","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3H5K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LE7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in PD-L1 and PD-L2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10213004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19014994","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in PD-L1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19014994","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
