6Q9R
Crystal structure of the pathological N184K variant of calcium-free human gelsolin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003779 | molecular_function | actin binding |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005546 | molecular_function | phosphatidylinositol-4,5-bisphosphate binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005925 | cellular_component | focal adhesion |
| A | 0006911 | biological_process | phagocytosis, engulfment |
| A | 0007015 | biological_process | actin filament organization |
| A | 0007417 | biological_process | central nervous system development |
| A | 0008154 | biological_process | actin polymerization or depolymerization |
| A | 0010628 | biological_process | positive regulation of gene expression |
| A | 0014891 | biological_process | striated muscle atrophy |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0016528 | cellular_component | sarcoplasm |
| A | 0030027 | cellular_component | lamellipodium |
| A | 0030030 | biological_process | cell projection organization |
| A | 0030031 | biological_process | cell projection assembly |
| A | 0030036 | biological_process | actin cytoskeleton organization |
| A | 0030041 | biological_process | actin filament polymerization |
| A | 0030042 | biological_process | actin filament depolymerization |
| A | 0030478 | cellular_component | actin cap |
| A | 0030864 | cellular_component | cortical actin cytoskeleton |
| A | 0031648 | biological_process | protein destabilization |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0035994 | biological_process | response to muscle stretch |
| A | 0036313 | molecular_function | phosphatidylinositol 3-kinase catalytic subunit binding |
| A | 0043065 | biological_process | positive regulation of apoptotic process |
| A | 0045159 | molecular_function | myosin II binding |
| A | 0045335 | cellular_component | phagocytic vesicle |
| A | 0046597 | biological_process | host-mediated suppression of symbiont invasion |
| 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 | 0051127 | biological_process | positive regulation of actin nucleation |
| A | 0051693 | biological_process | actin filament capping |
| A | 0055119 | biological_process | relaxation of cardiac muscle |
| A | 0060271 | biological_process | cilium assembly |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0072562 | cellular_component | blood microparticle |
| A | 0086003 | biological_process | cardiac muscle cell contraction |
| A | 0097017 | biological_process | renal protein absorption |
| A | 0097284 | biological_process | hepatocyte apoptotic process |
| A | 1902174 | biological_process | positive regulation of keratinocyte apoptotic process |
| A | 1903903 | biological_process | regulation of establishment of T cell polarity |
| A | 1903906 | biological_process | regulation of plasma membrane raft polarization |
| A | 1903909 | biological_process | regulation of receptor clustering |
| A | 1903923 | biological_process | positive regulation of protein processing in phagocytic vesicle |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| A | 1990000 | biological_process | amyloid fibril formation |
| B | 0003779 | molecular_function | actin binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005546 | molecular_function | phosphatidylinositol-4,5-bisphosphate binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005925 | cellular_component | focal adhesion |
| B | 0006911 | biological_process | phagocytosis, engulfment |
| B | 0007015 | biological_process | actin filament organization |
| B | 0007417 | biological_process | central nervous system development |
| B | 0008154 | biological_process | actin polymerization or depolymerization |
| B | 0010628 | biological_process | positive regulation of gene expression |
| B | 0014891 | biological_process | striated muscle atrophy |
| B | 0015629 | cellular_component | actin cytoskeleton |
| B | 0016528 | cellular_component | sarcoplasm |
| B | 0030027 | cellular_component | lamellipodium |
| B | 0030030 | biological_process | cell projection organization |
| B | 0030031 | biological_process | cell projection assembly |
| B | 0030036 | biological_process | actin cytoskeleton organization |
| B | 0030041 | biological_process | actin filament polymerization |
| B | 0030042 | biological_process | actin filament depolymerization |
| B | 0030478 | cellular_component | actin cap |
| B | 0030864 | cellular_component | cortical actin cytoskeleton |
| B | 0031648 | biological_process | protein destabilization |
| B | 0034774 | cellular_component | secretory granule lumen |
| B | 0035994 | biological_process | response to muscle stretch |
| B | 0036313 | molecular_function | phosphatidylinositol 3-kinase catalytic subunit binding |
| B | 0043065 | biological_process | positive regulation of apoptotic process |
| B | 0045159 | molecular_function | myosin II binding |
| B | 0045335 | cellular_component | phagocytic vesicle |
| B | 0046597 | biological_process | host-mediated suppression of symbiont invasion |
| 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 | 0051127 | biological_process | positive regulation of actin nucleation |
| B | 0051693 | biological_process | actin filament capping |
| B | 0055119 | biological_process | relaxation of cardiac muscle |
| B | 0060271 | biological_process | cilium assembly |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0072562 | cellular_component | blood microparticle |
| B | 0086003 | biological_process | cardiac muscle cell contraction |
| B | 0097017 | biological_process | renal protein absorption |
| B | 0097284 | biological_process | hepatocyte apoptotic process |
| B | 1902174 | biological_process | positive regulation of keratinocyte apoptotic process |
| B | 1903903 | biological_process | regulation of establishment of T cell polarity |
| B | 1903906 | biological_process | regulation of plasma membrane raft polarization |
| B | 1903909 | biological_process | regulation of receptor clustering |
| B | 1903923 | biological_process | positive regulation of protein processing in phagocytic vesicle |
| B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| B | 1990000 | biological_process | amyloid fibril formation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 801 |
| Chain | Residue |
| A | GLU126 |
| A | ARG172 |
| A | HOH959 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 802 |
| Chain | Residue |
| A | GLN409 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 803 |
| Chain | Residue |
| A | GLU31 |
| B | LYS34 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 804 |
| Chain | Residue |
| A | TYR453 |
| A | ARG458 |
| A | HOH985 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 806 |
| Chain | Residue |
| A | LYS503 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 807 |
| Chain | Residue |
| A | GLN540 |
| A | ARG542 |
| A | ASN562 |
| A | ARG629 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 808 |
| Chain | Residue |
| A | ASN196 |
| A | HOH935 |
| B | LYS150 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 809 |
| Chain | Residue |
| A | GLN364 |
| A | HIS638 |
| A | PRO639 |
| A | ARG641 |
| A | ASP675 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 810 |
| Chain | Residue |
| A | LYS503 |
| A | TRP677 |
| A | ASP678 |
| A | ARG711 |
| A | ASP712 |
| A | THR715 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 811 |
| Chain | Residue |
| A | GLN296 |
| A | LEU299 |
| A | GLU355 |
| A | GLU358 |
| A | TRP369 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 812 |
| Chain | Residue |
| A | LYS272 |
| A | HIS309 |
| A | GLY310 |
| A | LYS311 |
| A | TYR344 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 813 |
| Chain | Residue |
| A | ALA408 |
| A | GLN409 |
| A | GLY411 |
| A | THR676 |
| A | ASP678 |
| A | TRP732 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 814 |
| Chain | Residue |
| A | GLN496 |
| A | LYS693 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 815 |
| Chain | Residue |
| A | THR129 |
| A | PRO360 |
| A | TYR382 |
| A | SER384 |
| A | ARG641 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 816 |
| Chain | Residue |
| A | ARG207 |
| A | ARG210 |
| B | ARG207 |
| B | ARG210 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 801 |
| Chain | Residue |
| B | TYR87 |
| B | ARG120 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 802 |
| Chain | Residue |
| B | ARG542 |
| B | ARG629 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 804 |
| Chain | Residue |
| B | GLY723 |
| B | GLU725 |
| B | TRP736 |
| B | ASP738 |
| B | TRP741 |
| site_id | AE1 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 805 |
| Chain | Residue |
| B | ASP413 |
| B | ILE462 |
| B | TYR464 |
| B | PRO505 |
| B | GLN679 |
| B | PHE681 |
| B | THR718 |
| B | PRO726 |
| B | SER728 |
| B | HOH936 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 806 |
| Chain | Residue |
| B | LYS503 |
| B | TRP677 |
| B | ARG711 |
| B | ASP712 |
| B | THR715 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 807 |
| Chain | Residue |
| B | THR129 |
| B | THR359 |
| B | PRO360 |
| B | LEU361 |
| B | SER384 |
| B | ARG641 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 808 |
| Chain | Residue |
| B | GLN364 |
| B | HIS638 |
| B | PRO639 |
| B | ARG641 |
| B | ASP675 |
| B | TRP677 |
| site_id | AE5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 809 |
| Chain | Residue |
| B | ALA408 |
| B | GLN409 |
| B | LYS634 |
| B | THR676 |
| B | ASP678 |
| B | HOH946 |
| site_id | AE6 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 810 |
| Chain | Residue |
| B | LYS721 |
| B | LYS686 |
| B | LYS693 |
| site_id | AE7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 811 |
| Chain | Residue |
| B | TYR59 |
| B | TYR133 |
| B | PHE134 |
| B | LYS135 |
| site_id | AE8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 812 |
| Chain | Residue |
| B | GLN722 |
| B | GLY723 |
| B | TRP741 |
| B | HOH911 |
| site_id | AE9 |
| Number of Residues | 5 |
| Details | binding site for residue TRS B 813 |
| Chain | Residue |
| A | THR375 |
| A | ASP376 |
| B | THR417 |
| B | GLY418 |
| B | LYS420 |
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 | 132 |
| 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 | 76 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 30 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19666512","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FFK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16466744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16466744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16466744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphotyrosine; by SRC; in vitro","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| 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_FI19 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
