Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0051015 | molecular_function | actin filament binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0001725 | cellular_component | stress fiber |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005856 | cellular_component | cytoskeleton |
B | 0005865 | cellular_component | striated muscle thin filament |
B | 0005884 | cellular_component | actin filament |
B | 0015629 | cellular_component | actin cytoskeleton |
B | 0016787 | molecular_function | hydrolase activity |
B | 0030240 | biological_process | skeletal muscle thin filament assembly |
B | 0048741 | biological_process | skeletal muscle fiber development |
D | 0051015 | molecular_function | actin filament binding |
E | 0000166 | molecular_function | nucleotide binding |
E | 0001725 | cellular_component | stress fiber |
E | 0005515 | molecular_function | protein binding |
E | 0005524 | molecular_function | ATP binding |
E | 0005856 | cellular_component | cytoskeleton |
E | 0005865 | cellular_component | striated muscle thin filament |
E | 0005884 | cellular_component | actin filament |
E | 0015629 | cellular_component | actin cytoskeleton |
E | 0016787 | molecular_function | hydrolase activity |
E | 0030240 | biological_process | skeletal muscle thin filament assembly |
E | 0048741 | biological_process | skeletal muscle fiber development |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 401 |
Chain | Residue |
B | ATP400 |
B | HOH405 |
B | HOH406 |
B | HOH407 |
B | HOH408 |
B | HOH409 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 402 |
Chain | Residue |
A | VAL121 |
A | HOH513 |
A | GLY41 |
A | ASP42 |
A | GLU73 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 403 |
Chain | Residue |
A | ASP85 |
A | GLY90 |
A | ALA92 |
A | HOH486 |
A | HOH505 |
B | GLU169 |
B | HOH413 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 404 |
Chain | Residue |
B | SER325 |
B | HOH471 |
B | HOH472 |
B | HOH531 |
B | HOH572 |
D | GLU14 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA E 401 |
Chain | Residue |
E | ATP400 |
E | HOH408 |
E | HOH410 |
E | HOH411 |
E | HOH480 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 402 |
Chain | Residue |
D | GLY41 |
D | ASP42 |
D | GLU73 |
D | VAL121 |
D | HOH418 |
D | HOH455 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 403 |
Chain | Residue |
D | ASP85 |
D | GLY90 |
D | ALA92 |
D | HOH425 |
E | GLU169 |
E | HOH403 |
site_id | AC8 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE ATP B 400 |
Chain | Residue |
B | GLY15 |
B | SER16 |
B | GLY17 |
B | LEU18 |
B | LYS20 |
B | GLY158 |
B | ASP159 |
B | GLY160 |
B | VAL161 |
B | ARG212 |
B | LYS215 |
B | GLU216 |
B | GLY303 |
B | GLY304 |
B | THR305 |
B | MET307 |
B | TYR308 |
B | LYS338 |
B | CA401 |
B | HOH408 |
B | HOH409 |
B | HOH410 |
B | HOH411 |
B | HOH412 |
B | HOH478 |
B | HOH507 |
B | HOH551 |
site_id | AC9 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE ATP E 400 |
Chain | Residue |
E | GLY15 |
E | SER16 |
E | GLY17 |
E | LEU18 |
E | LYS20 |
E | GLY158 |
E | ASP159 |
E | GLY160 |
E | VAL161 |
E | GLY184 |
E | LYS215 |
E | GLU216 |
E | GLY303 |
E | GLY304 |
E | THR305 |
E | MET307 |
E | TYR308 |
E | LYS338 |
E | CA401 |
E | HOH408 |
E | HOH410 |
E | HOH412 |
E | HOH433 |
E | HOH484 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRS A 472 |
Chain | Residue |
A | TYR35 |
A | TYR109 |
A | PHE110 |
A | LYS111 |
A | SER112 |
E | ASN227 |
E | HOH454 |
Functional Information from PROSITE/UniProt
site_id | PS00406 |
Number of Residues | 11 |
Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
Chain | Residue | Details |
B | TYR55-GLY65 | |
site_id | PS00432 |
Number of Residues | 9 |
Details | ACTINS_2 Actins signature 2. WITKqEYDE |
Chain | Residue | Details |
B | TRP358-GLU366 | |
site_id | PS01132 |
Number of Residues | 13 |
Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
Chain | Residue | Details |
B | LEU106-ARG118 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 164 |
Details | Repeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 123 |
Details | Region: {"description":"Actin-severing","evidences":[{"evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Region: {"description":"Actin-actin interfilament contact point"} |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19666512","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FFK","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 14 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine; by SRC; in vitro","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"12356759","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MDU","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]} |