3DAW
Structure of the actin-depolymerizing factor homology domain in complex with actin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 |
| B | 0003779 | molecular_function | actin binding |
| B | 0030837 | biological_process | negative regulation of actin filament polymerization |
Functional Information from PDB Data
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP A 377 |
| Chain | Residue |
| A | GLY13 |
| A | LYS213 |
| A | GLU214 |
| A | GLY301 |
| A | GLY302 |
| A | THR303 |
| A | MET305 |
| A | TYR306 |
| A | LYS336 |
| A | SER14 |
| A | GLY15 |
| A | LEU16 |
| A | LYS18 |
| A | GLY156 |
| A | ASP157 |
| A | GLY158 |
| A | GLY182 |
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 | 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 | 2 |
| Details | Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| 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_FI5 |
| 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_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q5RJR2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18034455","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
