3SWL
Crystal Structure Analysis of H74A Mutant of Human CLIC1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005254 | molecular_function | chloride channel activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005634 | cellular_component | nucleus |
| A | 0005635 | cellular_component | nuclear envelope |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005903 | cellular_component | brush border |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006821 | biological_process | chloride transport |
| A | 0007165 | biological_process | signal transduction |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031965 | cellular_component | nuclear membrane |
| A | 0031982 | cellular_component | vesicle |
| A | 0034220 | biological_process | monoatomic ion transmembrane transport |
| A | 0034702 | cellular_component | monoatomic ion channel complex |
| A | 0034707 | cellular_component | chloride channel complex |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0045669 | biological_process | positive regulation of osteoblast differentiation |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0051881 | biological_process | regulation of mitochondrial membrane potential |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070527 | biological_process | platelet aggregation |
| A | 0072562 | cellular_component | blood microparticle |
| A | 1902476 | biological_process | chloride transmembrane transport |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Note=After insertion into the membrane","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 140 |
| Details | Domain: {"description":"GST C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00685","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Motif: {"description":"G-site","evidences":[{"source":"PubMed","id":"25581026","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11551966","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K0N","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"S-glutathionyl cysteine; alternate","evidences":[{"source":"PubMed","id":"14613939","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9Z1Q5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
