2ASP
Structure of Rabbit Actin In Complex With Reidispongiolide C
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 400 |
Chain | Residue |
A | ATP425 |
A | HOH767 |
A | HOH783 |
A | HOH787 |
A | HOH788 |
A | HOH886 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 600 |
Chain | Residue |
A | HOH743 |
A | HOH794 |
A | HOH805 |
A | HOH822 |
A | GLN263 |
A | SER265 |
A | EDO706 |
site_id | AC3 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE ATP A 425 |
Chain | Residue |
A | GLY13 |
A | SER14 |
A | GLY15 |
A | LEU16 |
A | LYS18 |
A | GLY156 |
A | ASP157 |
A | GLY158 |
A | VAL159 |
A | GLY182 |
A | ARG210 |
A | LYS213 |
A | GLU214 |
A | GLY301 |
A | GLY302 |
A | THR303 |
A | MET305 |
A | TYR306 |
A | LYS336 |
A | CA400 |
A | HOH756 |
A | HOH761 |
A | HOH767 |
A | HOH787 |
A | HOH788 |
A | HOH799 |
A | HOH800 |
A | HOH802 |
A | HOH807 |
A | HOH816 |
site_id | AC4 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE RGC A 500 |
Chain | Residue |
A | TYR91 |
A | ARG95 |
A | TYR143 |
A | ALA144 |
A | SER145 |
A | GLY146 |
A | ARG147 |
A | TYR169 |
A | PRO332 |
A | GLU334 |
A | SER338 |
A | ILE345 |
A | LEU346 |
A | ASP363 |
A | GLU364 |
A | ALA365 |
A | SER368 |
A | HOH755 |
A | HOH789 |
A | HOH936 |
A | HOH964 |
A | HOH988 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 700 |
Chain | Residue |
A | GLU224 |
A | ASN225 |
A | PHE262 |
A | GLN263 |
A | ARG312 |
A | GLU316 |
A | HOH795 |
A | HOH813 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 703 |
Chain | Residue |
A | ASN280 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 704 |
Chain | Residue |
A | GLN121 |
A | GLU125 |
A | TYR362 |
A | PRO367 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 705 |
Chain | Residue |
A | THR318 |
A | ALA319 |
A | ALA321 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 706 |
Chain | Residue |
A | ASN225 |
A | GLN263 |
A | SER265 |
A | CA600 |
A | HOH822 |
A | HOH1052 |
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 | 1 |
Details | MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665 |
Chain | Residue | Details |
A | ASP1 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134 |
Chain | Residue | Details |
A | MET44 | |
A | MET47 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS61 |
site_id | SWS_FT_FI4 |
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 |
A | HIS73 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
Chain | Residue | Details |
A | LYS84 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 |
Chain | Residue | Details |
A | ARG177 |