3CJC
Actin dimer cross-linked by V. cholerae MARTX toxin and complexed with DNase I and Gelsolin-segment 1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0001725 | cellular_component | stress fiber |
A | 0003785 | molecular_function | actin monomer binding |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005523 | molecular_function | tropomyosin binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005865 | cellular_component | striated muscle thin filament |
A | 0005884 | cellular_component | actin filament |
A | 0010628 | biological_process | positive regulation of gene expression |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019904 | molecular_function | protein domain specific binding |
A | 0030027 | cellular_component | lamellipodium |
A | 0030041 | biological_process | actin filament polymerization |
A | 0030175 | cellular_component | filopodium |
A | 0030240 | biological_process | skeletal muscle thin filament assembly |
A | 0031013 | molecular_function | troponin I binding |
A | 0031432 | molecular_function | titin binding |
A | 0031941 | cellular_component | filamentous actin |
A | 0032036 | molecular_function | myosin heavy chain binding |
A | 0032432 | cellular_component | actin filament bundle |
A | 0042802 | molecular_function | identical protein binding |
A | 0044297 | cellular_component | cell body |
A | 0048306 | molecular_function | calcium-dependent protein binding |
A | 0048741 | biological_process | skeletal muscle fiber development |
A | 0051017 | biological_process | actin filament bundle assembly |
A | 0090131 | biological_process | mesenchyme migration |
A | 0098723 | cellular_component | skeletal muscle myofibril |
A | 0140660 | molecular_function | cytoskeletal motor activator activity |
D | 0002283 | biological_process | neutrophil activation involved in immune response |
D | 0002673 | biological_process | regulation of acute inflammatory response |
D | 0003677 | molecular_function | DNA binding |
D | 0003779 | molecular_function | actin binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0004519 | molecular_function | endonuclease activity |
D | 0004530 | molecular_function | deoxyribonuclease I activity |
D | 0004536 | molecular_function | DNA nuclease activity |
D | 0005515 | molecular_function | protein binding |
D | 0005576 | cellular_component | extracellular region |
D | 0005634 | cellular_component | nucleus |
D | 0005635 | cellular_component | nuclear envelope |
D | 0006308 | biological_process | DNA catabolic process |
D | 0006915 | biological_process | apoptotic process |
D | 0031410 | cellular_component | cytoplasmic vesicle |
D | 0042588 | cellular_component | zymogen granule |
D | 0070948 | biological_process | regulation of neutrophil mediated cytotoxicity |
G | 0051015 | molecular_function | actin filament binding |
Functional Information from PROSITE/UniProt
site_id | PS00406 |
Number of Residues | 11 |
Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
Chain | Residue | Details |
A | TYR53-GLY63 |
site_id | PS00432 |
Number of Residues | 9 |
Details | ACTINS_2 Actins signature 2. WITKqEYDE |
Chain | Residue | Details |
A | TRP356-GLU364 |
site_id | PS00918 |
Number of Residues | 8 |
Details | DNASE_I_2 Deoxyribonuclease I signature 2. GDFNAdCS |
Chain | Residue | Details |
D | GLY167-SER174 |
site_id | PS00919 |
Number of Residues | 21 |
Details | DNASE_I_1 Deoxyribonuclease I signature 1. IVALHSAPsdavaEINsLyDV |
Chain | Residue | Details |
D | ILE130-VAL150 |
site_id | PS01132 |
Number of Residues | 13 |
Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
Chain | Residue | Details |
A | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK |
Chain | Residue | Details |
G | GLY41 | |
G | ASP42 | |
G | GLU73 | |
G | ASP85 | |
G | GLY90 | |
G | ALA92 | |
G | VAL121 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
G | LYS111 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by SRC; in vitro => ECO:0000269|PubMed:10210201 |
Chain | Residue | Details |
G | TYR35 | |
D | VAL67 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme |
Chain | Residue | Details |
D | TYR65 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1748997, ECO:0000269|PubMed:3560229 |
Chain | Residue | Details |
D | ASN18 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
Chain | Residue | Details |
A | LYS84 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 |
Chain | Residue | Details |
A | ARG177 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 41 |
Chain | Residue | Details |
D | GLU39 | metal ligand |
D | TYR76 | electrostatic stabiliser |
D | GLU78 | electrostatic stabiliser, increase acidity, increase basicity |
D | HIS134 | proton acceptor, proton donor |
D | ASP168 | metal ligand |
D | ASP212 | electrostatic stabiliser, increase acidity, increase basicity |
D | HIS252 | proton acceptor, proton donor |