25QP
Cryo-EM Structure of PLPP3
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 468 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 172 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"12660161","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 100 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"12660161","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 196 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"12660161","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 32 |
| Details | Region: {"description":"Phosphatase sequence motif I","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Region: {"description":"Phosphatase sequence motif II","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 44 |
| Details | Region: {"description":"Phosphatase sequence motif III","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Dityrosine basolateral targeting motif","evidences":[{"source":"PubMed","id":"14527693","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | Motif: {"description":"Integrin-binding motif","evidences":[{"source":"PubMed","id":"12660161","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16099422","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donors","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Site: {"description":"Stabilizes the active site histidine for nucleophilic attack","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
