1PJA
The crystal structure of palmitoyl protein thioesterase-2 reveals the basis for divergent substrate specificities of the two lysosomal thioesterases (PPT1 and PPT2)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0098599 | molecular_function | palmitoyl hydrolase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12855696","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"12855696","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12855696","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PJA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12855696, 10781062 |
| Chain | Residue | Details |
| A | SER111 | |
| A | ASP228 | |
| A | GLN112 | |
| A | LEU45 | |
| A | HIS283 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 523 |
| Chain | Residue | Details |
| A | LEU45 | electrostatic stabiliser |
| A | SER111 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLN112 | electrostatic stabiliser |
| A | ASP228 | electrostatic stabiliser, increase basicity |
| A | HIS283 | proton acceptor, proton donor |
