4B1X
Structure of the Phactr1 RPEL-2 bound to G-actin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0001725 | cellular_component | stress fiber |
| B | 0003785 | molecular_function | actin monomer binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005523 | molecular_function | tropomyosin 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 | 0010628 | biological_process | positive regulation of gene expression |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019904 | molecular_function | protein domain specific binding |
| B | 0030027 | cellular_component | lamellipodium |
| B | 0030041 | biological_process | actin filament polymerization |
| B | 0030175 | cellular_component | filopodium |
| B | 0030240 | biological_process | skeletal muscle thin filament assembly |
| B | 0031013 | molecular_function | troponin I binding |
| B | 0031432 | molecular_function | titin binding |
| B | 0031941 | cellular_component | filamentous actin |
| B | 0032036 | molecular_function | myosin heavy chain binding |
| B | 0032432 | cellular_component | actin filament bundle |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0044297 | cellular_component | cell body |
| B | 0048306 | molecular_function | calcium-dependent protein binding |
| B | 0048741 | biological_process | skeletal muscle fiber development |
| B | 0051017 | biological_process | actin filament bundle assembly |
| B | 0090131 | biological_process | mesenchyme migration |
| B | 0098723 | cellular_component | skeletal muscle myofibril |
| B | 0140660 | molecular_function | cytoskeletal motor activator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LAB B 1376 |
| Chain | Residue |
| B | GLY15 |
| B | ARG210 |
| B | HOH2118 |
| B | LEU16 |
| B | GLN59 |
| B | TYR69 |
| B | ASP157 |
| B | ARG183 |
| B | THR186 |
| B | ARG206 |
| B | GLU207 |
| site_id | AC2 |
| Number of Residues | 28 |
| 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 | MG1378 |
| B | HOH2005 |
| B | HOH2008 |
| B | HOH2011 |
| B | HOH2078 |
| B | HOH2079 |
| B | HOH2117 |
| B | HOH2196 |
| M | HOH2013 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1378 |
| Chain | Residue |
| B | ATP1377 |
| B | HOH2004 |
| B | HOH2005 |
| B | HOH2078 |
| B | HOH2196 |
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-ARG498 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9C0D0 |
| Chain | Residue | Details |
| M | SER467 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665 |
| Chain | Residue | Details |
| B | ASP1 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134 |
| Chain | Residue | Details |
| B | MET44 | |
| B | MET47 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
| Chain | Residue | Details |
| B | LYS61 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK |
| Chain | Residue | Details |
| B | HIS73 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
| Chain | Residue | Details |
| B | LYS84 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 |
| Chain | Residue | Details |
| B | ARG177 |
