4B1U
Structure of the Phactr1 RPEL domain and RPEL motif directed assemblies with G-actin reveal the molecular basis for actin binding cooperativity.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0001725 | cellular_component | stress fiber |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0005865 | cellular_component | striated muscle thin filament |
| B | 0005884 | cellular_component | actin filament |
| B | 0009612 | biological_process | response to mechanical stimulus |
| B | 0010628 | biological_process | positive regulation of gene expression |
| B | 0015629 | cellular_component | actin cytoskeleton |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030017 | cellular_component | sarcomere |
| B | 0030027 | cellular_component | lamellipodium |
| B | 0030175 | cellular_component | filopodium |
| B | 0030240 | biological_process | skeletal muscle thin filament assembly |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0035865 | biological_process | cellular response to potassium ion |
| B | 0043503 | biological_process | skeletal muscle fiber adaptation |
| B | 0044297 | cellular_component | cell body |
| B | 0048545 | biological_process | response to steroid hormone |
| B | 0048741 | biological_process | skeletal muscle fiber development |
| B | 0090131 | biological_process | mesenchyme migration |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE LAB B 1376 |
| Chain | Residue |
| B | GLY15 |
| B | THR186 |
| B | ARG206 |
| B | GLU207 |
| B | ARG210 |
| B | ATP1377 |
| B | HOH2103 |
| B | LEU16 |
| B | PRO32 |
| B | ILE34 |
| B | GLN59 |
| B | TYR69 |
| B | ASP157 |
| B | GLY182 |
| B | ARG183 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE ATP B 1377 |
| Chain | Residue |
| B | GLY13 |
| B | SER14 |
| B | GLY15 |
| B | LEU16 |
| B | LYS18 |
| B | GLY156 |
| B | ASP157 |
| B | GLY158 |
| B | VAL159 |
| B | GLY182 |
| B | ARG210 |
| B | LYS213 |
| B | GLU214 |
| B | GLY301 |
| B | GLY302 |
| B | THR303 |
| B | MET305 |
| B | TYR306 |
| B | LYS336 |
| B | LAB1376 |
| B | MG1378 |
| B | HOH2004 |
| B | HOH2005 |
| B | HOH2013 |
| B | HOH2061 |
| B | HOH2077 |
| B | HOH2100 |
| B | HOH2101 |
| B | HOH2147 |
| B | HOH2148 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1378 |
| Chain | Residue |
| B | ATP1377 |
| B | HOH2002 |
| B | HOH2004 |
| B | HOH2061 |
| B | HOH2148 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TRS B 1379 |
| Chain | Residue |
| B | HIS73 |
| B | ASP179 |
| B | HOH2086 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA M 1163 |
| Chain | Residue |
| M | PHE133 |
| M | LYS134 |
| M | HIS135 |
| M | THR136 |
Functional Information from PROSITE/UniProt
| site_id | PS00406 |
| Number of Residues | 11 |
| Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
| Chain | Residue | Details |
| B | TYR53-GLY63 |
| site_id | PS00432 |
| Number of Residues | 9 |
| Details | ACTINS_2 Actins signature 2. WITKqEYDE |
| Chain | Residue | Details |
| B | TRP356-GLU364 |
| site_id | PS01132 |
| Number of Residues | 13 |
| Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
| Chain | Residue | Details |
| B | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000269|PubMed:36173861 |
| Chain | Residue | Details |
| B | CYS0 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Methionine (R)-sulfoxide => ECO:0000269|PubMed:23911929 |
| Chain | Residue | Details |
| B | MET44 | |
| B | MET47 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
| Chain | Residue | Details |
| B | LYS61 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Tele-methylhistidine => ECO:0000250|UniProtKB:P68138 |
| Chain | Residue | Details |
| B | HIS73 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
| Chain | Residue | Details |
| B | LYS84 |
