1RDW
Actin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| X | 0000166 | molecular_function | nucleotide binding |
| X | 0000287 | molecular_function | magnesium ion binding |
| X | 0001725 | cellular_component | stress fiber |
| X | 0003785 | molecular_function | actin monomer binding |
| X | 0005509 | molecular_function | calcium ion binding |
| X | 0005515 | molecular_function | protein binding |
| X | 0005523 | molecular_function | tropomyosin binding |
| X | 0005524 | molecular_function | ATP binding |
| X | 0005737 | cellular_component | cytoplasm |
| X | 0005856 | cellular_component | cytoskeleton |
| X | 0005865 | cellular_component | striated muscle thin filament |
| X | 0005884 | cellular_component | actin filament |
| X | 0010628 | biological_process | positive regulation of gene expression |
| X | 0016787 | molecular_function | hydrolase activity |
| X | 0019904 | molecular_function | protein domain specific binding |
| X | 0030027 | cellular_component | lamellipodium |
| X | 0030041 | biological_process | actin filament polymerization |
| X | 0030175 | cellular_component | filopodium |
| X | 0030240 | biological_process | skeletal muscle thin filament assembly |
| X | 0031013 | molecular_function | troponin I binding |
| X | 0031432 | molecular_function | titin binding |
| X | 0031941 | cellular_component | filamentous actin |
| X | 0032036 | molecular_function | myosin heavy chain binding |
| X | 0032432 | cellular_component | actin filament bundle |
| X | 0042802 | molecular_function | identical protein binding |
| X | 0044297 | cellular_component | cell body |
| X | 0048306 | molecular_function | calcium-dependent protein binding |
| X | 0048741 | biological_process | skeletal muscle fiber development |
| X | 0051017 | biological_process | actin filament bundle assembly |
| X | 0090131 | biological_process | mesenchyme migration |
| X | 0098723 | cellular_component | skeletal muscle myofibril |
| X | 0140660 | molecular_function | cytoskeletal motor activator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG X 392 |
| Chain | Residue |
| X | ATP390 |
| X | HOH423 |
| X | HOH424 |
| X | HOH425 |
| X | HOH426 |
| X | HOH472 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ATP X 390 |
| Chain | Residue |
| X | LEU16 |
| X | LYS18 |
| X | GLY156 |
| X | ASP157 |
| X | GLY158 |
| X | VAL159 |
| X | GLY182 |
| X | ARG210 |
| X | LYS213 |
| X | GLU214 |
| X | GLY301 |
| X | GLY302 |
| X | THR303 |
| X | MET305 |
| X | TYR306 |
| X | LAR391 |
| X | MG392 |
| X | HOH401 |
| X | HOH404 |
| X | HOH419 |
| X | HOH425 |
| X | HOH426 |
| X | HOH440 |
| X | HOH460 |
| X | HOH472 |
| X | GLY13 |
| X | SER14 |
| X | GLY15 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LAR X 391 |
| Chain | Residue |
| X | GLY15 |
| X | LEU16 |
| X | GLN59 |
| X | TYR69 |
| X | ASP157 |
| X | ARG183 |
| X | THR186 |
| X | ARG206 |
| X | GLU207 |
| X | ARG210 |
| X | LYS213 |
| X | ATP390 |
| X | HOH474 |
Functional Information from PROSITE/UniProt
| site_id | PS00406 |
| Number of Residues | 11 |
| Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
| Chain | Residue | Details |
| X | TYR53-GLY63 |
| site_id | PS00432 |
| Number of Residues | 9 |
| Details | ACTINS_2 Actins signature 2. WITKqEYDE |
| Chain | Residue | Details |
| X | TRP356-GLU364 |
| site_id | PS01132 |
| Number of Residues | 13 |
| Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
| Chain | Residue | Details |
| X | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 25 |
| Details | Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
