4B1V
Structure of the Phactr1 RPEL-N domain bound to G-actin
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 30 |
Details | BINDING SITE FOR RESIDUE ATP A 1377 |
Chain | Residue |
A | GLY13 |
A | GLY182 |
A | ARG210 |
A | LYS213 |
A | GLU214 |
A | GLY301 |
A | GLY302 |
A | THR303 |
A | MET305 |
A | TYR306 |
A | MG1378 |
A | SER14 |
A | HOH2002 |
A | HOH2003 |
A | HOH2006 |
A | HOH2012 |
A | HOH2094 |
A | HOH2110 |
A | HOH2166 |
A | HOH2167 |
A | HOH2280 |
A | HOH2281 |
A | GLY15 |
A | HOH2282 |
A | LEU16 |
A | LYS18 |
A | GLY156 |
A | ASP157 |
A | GLY158 |
A | VAL159 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1378 |
Chain | Residue |
A | ATP1377 |
A | HOH2002 |
A | HOH2003 |
A | HOH2094 |
A | HOH2281 |
site_id | AC3 |
Number of Residues | 29 |
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 | MG1378 |
B | HOH2003 |
B | HOH2005 |
B | HOH2006 |
B | HOH2011 |
B | HOH2100 |
B | HOH2120 |
B | HOH2174 |
B | HOH2175 |
B | HOH2270 |
B | HOH2283 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 1378 |
Chain | Residue |
B | ATP1377 |
B | HOH2003 |
B | HOH2005 |
B | HOH2100 |
B | HOH2283 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 1501 |
Chain | Residue |
B | GLY23 |
B | ASP24 |
B | ASP25 |
B | ILE345 |
B | SER348 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 1502 |
Chain | Residue |
B | THR203 |
B | GOL1506 |
B | HOH2160 |
B | HOH2285 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 1503 |
Chain | Residue |
A | VAL96 |
B | HIS87 |
B | TYR91 |
B | PHE127 |
B | HOH2051 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 1504 |
Chain | Residue |
B | TYR133 |
B | TYR143 |
B | PHE375 |
B | HOH2097 |
N | ARG147 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1501 |
Chain | Residue |
A | TYR133 |
A | TYR143 |
A | PHE375 |
A | HOH2092 |
M | ARG147 |
site_id | BC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE LAB A 1500 |
Chain | Residue |
A | ARG183 |
A | THR186 |
A | GLU207 |
A | ARG210 |
A | HOH2170 |
A | GLY15 |
A | LEU16 |
A | GLN59 |
A | TYR69 |
A | ASP157 |
A | GLY182 |
site_id | BC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE LAB B 1500 |
Chain | Residue |
B | GLY15 |
B | LEU16 |
B | GLN59 |
B | TYR69 |
B | ASP157 |
B | ARG183 |
B | THR186 |
B | ARG206 |
B | GLU207 |
B | ARG210 |
B | LYS213 |
B | HOH2177 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 1506 |
Chain | Residue |
B | MET190 |
B | VAL201 |
B | THR202 |
B | ARG206 |
B | EDO1502 |
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 | 2 |
Details | MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737 |
Chain | Residue | Details |
A | CYS0 | |
B | CYS0 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665 |
Chain | Residue | Details |
A | ASP1 | |
B | ASP1 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134 |
Chain | Residue | Details |
A | MET44 | |
A | MET47 | |
B | MET44 | |
B | MET47 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS61 | |
B | LYS61 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
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 |
A | HIS73 | |
B | HIS73 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
Chain | Residue | Details |
A | LYS84 | |
B | LYS84 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 |
Chain | Residue | Details |
A | ARG177 | |
B | ARG177 |