3FFK
Crystal structure of human Gelsolin domains G1-G3 bound to Actin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0051015 | molecular_function | actin filament binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0001725 | cellular_component | stress fiber |
B | 0003785 | molecular_function | actin monomer binding |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005523 | molecular_function | tropomyosin binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005856 | cellular_component | cytoskeleton |
B | 0005865 | cellular_component | striated muscle thin filament |
B | 0005884 | cellular_component | actin filament |
B | 0010628 | biological_process | positive regulation of gene expression |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019904 | molecular_function | protein domain specific binding |
B | 0030027 | cellular_component | lamellipodium |
B | 0030041 | biological_process | actin filament polymerization |
B | 0030175 | cellular_component | filopodium |
B | 0030240 | biological_process | skeletal muscle thin filament assembly |
B | 0031013 | molecular_function | troponin I binding |
B | 0031432 | molecular_function | titin binding |
B | 0031941 | cellular_component | filamentous actin |
B | 0032036 | molecular_function | myosin heavy chain binding |
B | 0032432 | cellular_component | actin filament bundle |
B | 0042802 | molecular_function | identical protein binding |
B | 0044297 | cellular_component | cell body |
B | 0048306 | molecular_function | calcium-dependent protein binding |
B | 0048741 | biological_process | skeletal muscle fiber development |
B | 0051017 | biological_process | actin filament bundle assembly |
B | 0090131 | biological_process | mesenchyme migration |
B | 0098723 | cellular_component | skeletal muscle myofibril |
B | 0140660 | molecular_function | cytoskeletal motor activator activity |
D | 0051015 | molecular_function | actin filament binding |
E | 0000287 | molecular_function | magnesium ion binding |
E | 0001725 | cellular_component | stress fiber |
E | 0003785 | molecular_function | actin monomer binding |
E | 0005509 | molecular_function | calcium ion binding |
E | 0005515 | molecular_function | protein binding |
E | 0005523 | molecular_function | tropomyosin binding |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005856 | cellular_component | cytoskeleton |
E | 0005865 | cellular_component | striated muscle thin filament |
E | 0005884 | cellular_component | actin filament |
E | 0010628 | biological_process | positive regulation of gene expression |
E | 0016787 | molecular_function | hydrolase activity |
E | 0019904 | molecular_function | protein domain specific binding |
E | 0030027 | cellular_component | lamellipodium |
E | 0030041 | biological_process | actin filament polymerization |
E | 0030175 | cellular_component | filopodium |
E | 0030240 | biological_process | skeletal muscle thin filament assembly |
E | 0031013 | molecular_function | troponin I binding |
E | 0031432 | molecular_function | titin binding |
E | 0031941 | cellular_component | filamentous actin |
E | 0032036 | molecular_function | myosin heavy chain binding |
E | 0032432 | cellular_component | actin filament bundle |
E | 0042802 | molecular_function | identical protein binding |
E | 0044297 | cellular_component | cell body |
E | 0048306 | molecular_function | calcium-dependent protein binding |
E | 0048741 | biological_process | skeletal muscle fiber development |
E | 0051017 | biological_process | actin filament bundle assembly |
E | 0090131 | biological_process | mesenchyme migration |
E | 0098723 | cellular_component | skeletal muscle myofibril |
E | 0140660 | molecular_function | cytoskeletal motor activator activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 756 |
Chain | Residue |
A | GLY186 |
A | ASP187 |
A | GLU209 |
A | ASP259 |
A | HOH789 |
A | HOH883 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 757 |
Chain | Residue |
A | VAL145 |
A | GLY65 |
A | ASP66 |
A | GLU97 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 758 |
Chain | Residue |
A | ASP109 |
A | GLY114 |
A | ALA116 |
A | HOH853 |
A | HOH882 |
B | GLU167 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 759 |
Chain | Residue |
A | GLU302 |
A | ASP303 |
A | GLU327 |
A | HOH777 |
A | HOH802 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 401 |
Chain | Residue |
B | ATP380 |
B | HOH392 |
B | HOH398 |
B | HOH469 |
B | HOH470 |
site_id | AC6 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ATP B 380 |
Chain | Residue |
B | GLY13 |
B | SER14 |
B | GLY15 |
B | LEU16 |
B | LYS18 |
B | GLY156 |
B | ASP157 |
B | GLY158 |
B | VAL159 |
B | GLY182 |
B | ARG210 |
B | LYS213 |
B | GLU214 |
B | GLY301 |
B | GLY302 |
B | THR303 |
B | MET305 |
B | TYR306 |
B | HOH379 |
B | HOH392 |
B | CA401 |
B | HOH470 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 756 |
Chain | Residue |
D | GLY186 |
D | ASP187 |
D | GLU209 |
D | ASP259 |
D | HOH784 |
D | HOH852 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA D 757 |
Chain | Residue |
D | GLY65 |
D | ASP66 |
D | GLU97 |
D | VAL145 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA D 758 |
Chain | Residue |
D | ASP109 |
D | GLY114 |
D | ALA116 |
D | HOH833 |
E | GLU167 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA D 759 |
Chain | Residue |
D | GLU302 |
D | ASP303 |
D | GLU327 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA E 401 |
Chain | Residue |
E | ATP380 |
E | HOH395 |
E | HOH433 |
E | HOH441 |
E | HOH490 |
site_id | BC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ATP E 380 |
Chain | Residue |
E | GLY13 |
E | SER14 |
E | GLY15 |
E | LEU16 |
E | LYS18 |
E | GLY156 |
E | ASP157 |
E | GLY158 |
E | VAL159 |
E | GLY182 |
E | LYS213 |
E | GLU214 |
E | GLY301 |
E | GLY302 |
E | THR303 |
E | MET305 |
E | TYR306 |
E | HOH395 |
E | CA401 |
E | HOH440 |
E | HOH450 |
E | HOH490 |
E | HOH495 |
Functional Information from PROSITE/UniProt
site_id | PS00406 |
Number of Residues | 11 |
Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
Chain | Residue | Details |
B | TYR53-GLY63 |
site_id | PS00432 |
Number of Residues | 9 |
Details | ACTINS_2 Actins signature 2. WITKqEYDE |
Chain | Residue | Details |
B | TRP356-GLU364 |
site_id | PS01132 |
Number of Residues | 13 |
Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
Chain | Residue | Details |
B | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737 |
Chain | Residue | Details |
B | CYS0 | |
A | GLU209 | |
A | ASP259 | |
A | GLU302 | |
A | ASP303 | |
A | GLU327 | |
D | GLY65 | |
D | ASP66 | |
D | GLU97 | |
D | ASP109 | |
D | GLY114 | |
E | CYS0 | |
D | ALA116 | |
D | VAL145 | |
D | GLY186 | |
D | ASP187 | |
D | GLU209 | |
D | ASP259 | |
D | GLU302 | |
D | ASP303 | |
D | GLU327 | |
A | GLU97 | |
A | ASP109 | |
A | GLY114 | |
A | ALA116 | |
A | VAL145 | |
A | GLY186 | |
A | ASP187 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665 |
Chain | Residue | Details |
B | ASP1 | |
E | ASP1 | |
D | LYS135 | |
D | ARG161 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134 |
Chain | Residue | Details |
B | MET44 | |
B | MET47 | |
E | MET44 | |
E | MET47 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
Chain | Residue | Details |
B | LYS61 | |
E | LYS61 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK |
Chain | Residue | Details |
B | HIS73 | |
E | HIS73 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
Chain | Residue | Details |
B | LYS84 | |
E | LYS84 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 |
Chain | Residue | Details |
B | ARG177 | |
E | ARG177 |