2WE6
Crystal Structure of Plasmodium falciparum Ubiquitin Carboxyl- terminal Hydrolase 3 (UCHL3)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000151 | cellular_component | ubiquitin ligase complex |
| A | 0000338 | biological_process | protein deneddylation |
| A | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006508 | biological_process | proteolysis |
| A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| A | 0016579 | biological_process | protein deubiquitination |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019784 | molecular_function | deNEDDylase activity |
| A | 0030163 | biological_process | protein catabolic process |
| A | 0043130 | molecular_function | ubiquitin binding |
| B | 0000151 | cellular_component | ubiquitin ligase complex |
| B | 0000338 | biological_process | protein deneddylation |
| B | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006508 | biological_process | proteolysis |
| B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008234 | molecular_function | cysteine-type peptidase activity |
| B | 0016579 | biological_process | protein deubiquitination |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019784 | molecular_function | deNEDDylase activity |
| B | 0030163 | biological_process | protein catabolic process |
| B | 0043130 | molecular_function | ubiquitin binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Region: {"description":"Interaction with ubiquitin","evidences":[{"source":"PubMed","id":"20042598","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Region: {"description":"Crossover loop which restricts access of large ubiquitin adducts to the active site","evidences":[{"source":"PubMed","id":"19047059","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20042598","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Site: {"description":"Interaction with ubiquitin","evidences":[{"source":"PubMed","id":"20042598","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for enzyme activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uch |
| Chain | Residue | Details |
| A | ASP179 | |
| A | HIS164 | |
| A | CYS92 | |
| A | GLN86 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uch |
| Chain | Residue | Details |
| B | ASP179 | |
| B | HIS164 | |
| B | CYS92 | |
| B | GLN86 |
