4FO0
Human actin-related protein Arp8 in its ATP-bound state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000723 | biological_process | telomere maintenance |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005694 | cellular_component | chromosome |
A | 0005813 | cellular_component | centrosome |
A | 0006275 | biological_process | regulation of DNA replication |
A | 0006281 | biological_process | DNA repair |
A | 0006282 | biological_process | regulation of DNA repair |
A | 0006302 | biological_process | double-strand break repair |
A | 0006310 | biological_process | DNA recombination |
A | 0006338 | biological_process | chromatin remodeling |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0031011 | cellular_component | Ino80 complex |
A | 0033044 | biological_process | regulation of chromosome organization |
A | 0045739 | biological_process | positive regulation of DNA repair |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
A | 0045995 | biological_process | regulation of embryonic development |
A | 0051301 | biological_process | cell division |
A | 0051726 | biological_process | regulation of cell cycle |
A | 0060382 | biological_process | regulation of DNA strand elongation |
A | 1904507 | biological_process | positive regulation of telomere maintenance in response to DNA damage |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 701 |
Chain | Residue |
A | LYS288 |
A | ATP702 |
A | HOH844 |
A | HOH901 |
A | HOH905 |
A | HOH907 |
site_id | AC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE ATP A 702 |
Chain | Residue |
A | THR57 |
A | ARG59 |
A | GLY285 |
A | ASP286 |
A | GLN287 |
A | LYS288 |
A | GLY311 |
A | GLN344 |
A | LYS347 |
A | GLU348 |
A | GLY539 |
A | GLY540 |
A | GLY541 |
A | MET543 |
A | PHE544 |
A | MG701 |
A | HOH809 |
A | HOH813 |
A | HOH814 |
A | HOH815 |
A | HOH844 |
A | HOH845 |
A | HOH901 |
A | HOH930 |
A | GLY54 |
A | SER55 |
A | THR56 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 703 |
Chain | Residue |
A | GLN105 |
A | PRO395 |
A | ALA396 |
A | PHE398 |
A | GLY399 |
A | ILE400 |
A | MET405 |
A | ALA508 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 704 |
Chain | Residue |
A | GLY153 |
A | ASN154 |
A | LYS155 |
A | TYR173 |
A | HOH823 |
A | HOH940 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 705 |
Chain | Residue |
A | GLN107 |
A | LEU110 |
A | LYS111 |
A | ASP114 |
A | ASP149 |
A | HIS150 |
A | HOH871 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 706 |
Chain | Residue |
A | TYR329 |
A | GLU331 |
A | GLN333 |
A | ASP339 |
A | HOH939 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 707 |
Chain | Residue |
A | PHE350 |
A | HIS363 |
A | LYS385 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 708 |
Chain | Residue |
A | TRP156 |
A | THR157 |
A | ASN158 |
A | THR159 |
A | SER160 |
A | ASN175 |
A | ASP178 |
A | HOH919 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 709 |
Chain | Residue |
A | PRO176 |
A | THR335 |
A | ASN336 |
A | LYS337 |
A | MET338 |
A | HOH842 |
A | HOH929 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 710 |
Chain | Residue |
A | GLN44 |
A | GLN44 |
A | SER45 |
A | ALA593 |
A | CYS594 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 711 |
Chain | Residue |
A | MET579 |
A | ASP580 |
A | LYS587 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | SER55 | |
A | THR56 | |
A | ASP283 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER132 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER412 |