1D0N
THE CRYSTAL STRUCTURE OF CALCIUM-FREE EQUINE PLASMA GELSOLIN.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003779 | molecular_function | actin binding |
| A | 0005546 | molecular_function | phosphatidylinositol-4,5-bisphosphate binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0007015 | biological_process | actin filament organization |
| A | 0007417 | biological_process | central nervous system development |
| A | 0008154 | biological_process | actin polymerization or depolymerization |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0030030 | biological_process | cell projection organization |
| A | 0030031 | biological_process | cell projection assembly |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051014 | biological_process | actin filament severing |
| A | 0051015 | molecular_function | actin filament binding |
| A | 0051016 | biological_process | barbed-end actin filament capping |
| A | 0051693 | biological_process | actin filament capping |
| A | 0060271 | biological_process | cilium assembly |
| B | 0003779 | molecular_function | actin binding |
| B | 0005546 | molecular_function | phosphatidylinositol-4,5-bisphosphate binding |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0007015 | biological_process | actin filament organization |
| B | 0007417 | biological_process | central nervous system development |
| B | 0008154 | biological_process | actin polymerization or depolymerization |
| B | 0015629 | cellular_component | actin cytoskeleton |
| B | 0030030 | biological_process | cell projection organization |
| B | 0030031 | biological_process | cell projection assembly |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051014 | biological_process | actin filament severing |
| B | 0051015 | molecular_function | actin filament binding |
| B | 0051016 | biological_process | barbed-end actin filament capping |
| B | 0051693 | biological_process | actin filament capping |
| B | 0060271 | biological_process | cilium assembly |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 164 |
| Details | Repeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 144 |
| Details | Repeat: {"description":"Gelsolin-like 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 144 |
| Details | Repeat: {"description":"Gelsolin-like 3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 162 |
| Details | Repeat: {"description":"Gelsolin-like 4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 116 |
| Details | Repeat: {"description":"Gelsolin-like 5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 150 |
| Details | Repeat: {"description":"Gelsolin-like 6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Region: {"description":"Actin-actin interfilament contact point"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 696 |
| Details | Region: {"description":"Actin-binding, Ca-sensitive","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15215896","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RGI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 34 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P06396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P13020","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P06396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
