1EQY
COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 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 |
S | 0051015 | molecular_function | actin filament binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 385 |
Chain | Residue |
A | ATP380 |
A | HOH1227 |
A | HOH1228 |
A | HOH1229 |
A | HOH1230 |
A | HOH1231 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA S 390 |
Chain | Residue |
S | ALA92 |
S | HOH951 |
S | HOH1015 |
S | HOH1232 |
A | GLU167 |
S | ASP85 |
S | GLY90 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA S 395 |
Chain | Residue |
S | GLY41 |
S | ASP42 |
S | GLU73 |
S | VAL121 |
S | HOH1233 |
S | HOH1234 |
site_id | AC4 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ATP A 380 |
Chain | Residue |
A | GLY13 |
A | SER14 |
A | GLY15 |
A | LEU16 |
A | LYS18 |
A | GLY156 |
A | ASP157 |
A | GLY158 |
A | VAL159 |
A | GLY182 |
A | LYS213 |
A | GLU214 |
A | GLY302 |
A | THR303 |
A | MET305 |
A | CA385 |
A | HOH813 |
A | HOH836 |
A | HOH886 |
A | HOH940 |
A | HOH965 |
A | HOH1228 |
A | HOH1231 |
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 | 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 | 1 |
Details | MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737 |
Chain | Residue | Details |
A | CYS0 | |
S | ASP42 | |
S | GLU73 | |
S | ASP85 | |
S | GLY90 | |
S | ALA92 | |
S | VAL121 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665 |
Chain | Residue | Details |
A | ASP1 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134 |
Chain | Residue | Details |
A | MET44 | |
A | MET47 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS61 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
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 |
A | HIC73 |
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 |