7W4Z
Crystal structure of fragmin domain-1 in complex with actin (AMPPNP-form)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0001725 | cellular_component | stress fiber |
A | 0005515 | molecular_function | protein 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 | 0015629 | cellular_component | actin cytoskeleton |
A | 0016787 | molecular_function | hydrolase activity |
A | 0030240 | biological_process | skeletal muscle thin filament assembly |
A | 0048741 | biological_process | skeletal muscle fiber development |
B | 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 | 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 | Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"12356759","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MDU","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |