5YPU
Crystal structure of an actin monomer in complex with the nucleator Cordon-Bleu MET72NLE WH2-motif peptide
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 | 0003779 | molecular_function | actin binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0001725 | cellular_component | stress fiber |
C | 0003785 | molecular_function | actin monomer binding |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0005523 | molecular_function | tropomyosin binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005856 | cellular_component | cytoskeleton |
C | 0005865 | cellular_component | striated muscle thin filament |
C | 0005884 | cellular_component | actin filament |
C | 0010628 | biological_process | positive regulation of gene expression |
C | 0016787 | molecular_function | hydrolase activity |
C | 0019904 | molecular_function | protein domain specific binding |
C | 0030027 | cellular_component | lamellipodium |
C | 0030041 | biological_process | actin filament polymerization |
C | 0030175 | cellular_component | filopodium |
C | 0030240 | biological_process | skeletal muscle thin filament assembly |
C | 0031013 | molecular_function | troponin I binding |
C | 0031432 | molecular_function | titin binding |
C | 0031941 | cellular_component | filamentous actin |
C | 0032036 | molecular_function | myosin heavy chain binding |
C | 0032432 | cellular_component | actin filament bundle |
C | 0042802 | molecular_function | identical protein binding |
C | 0044297 | cellular_component | cell body |
C | 0048306 | molecular_function | calcium-dependent protein binding |
C | 0048741 | biological_process | skeletal muscle fiber development |
C | 0051017 | biological_process | actin filament bundle assembly |
C | 0090131 | biological_process | mesenchyme migration |
C | 0098723 | cellular_component | skeletal muscle myofibril |
C | 0140660 | molecular_function | cytoskeletal motor activator activity |
D | 0003779 | molecular_function | actin binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | binding site for residue ATP A 401 |
Chain | Residue |
A | GLY13 |
A | GLY182 |
A | ARG210 |
A | LYS213 |
A | GLU214 |
A | GLY301 |
A | GLY302 |
A | THR303 |
A | MET305 |
A | TYR306 |
A | CA402 |
A | SER14 |
A | HOH586 |
A | HOH604 |
A | HOH615 |
A | HOH627 |
A | HOH634 |
A | HOH660 |
A | HOH689 |
A | HOH708 |
A | GLY15 |
A | LEU16 |
A | LYS18 |
A | GLY156 |
A | ASP157 |
A | GLY158 |
A | VAL159 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 402 |
Chain | Residue |
A | ATP401 |
A | HOH541 |
A | HOH565 |
A | HOH576 |
A | HOH615 |
A | HOH708 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA A 403 |
Chain | Residue |
A | ASP286 |
A | ASP288 |
A | ASP363 |
A | HOH569 |
A | HOH674 |
A | HOH678 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue CA B 101 |
Chain | Residue |
A | ASP187 |
A | HOH573 |
A | HOH717 |
A | HOH730 |
B | GLU82 |
B | HOH208 |
B | HOH213 |
site_id | AC5 |
Number of Residues | 27 |
Details | binding site for residue ATP C 401 |
Chain | Residue |
C | GLY13 |
C | SER14 |
C | GLY15 |
C | LEU16 |
C | LYS18 |
C | GLY156 |
C | ASP157 |
C | GLY158 |
C | VAL159 |
C | GLY182 |
C | ARG210 |
C | LYS213 |
C | GLU214 |
C | GLY301 |
C | GLY302 |
C | THR303 |
C | MET305 |
C | TYR306 |
C | CA402 |
C | HOH574 |
C | HOH586 |
C | HOH589 |
C | HOH599 |
C | HOH604 |
C | HOH611 |
C | HOH622 |
C | HOH680 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CA C 402 |
Chain | Residue |
C | ATP401 |
C | HOH539 |
C | HOH552 |
C | HOH559 |
C | HOH586 |
C | HOH622 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue CA C 403 |
Chain | Residue |
C | ASP286 |
C | ASP288 |
C | ASP363 |
C | HOH571 |
C | HOH674 |
C | HOH675 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CA C 404 |
Chain | Residue |
A | HOH581 |
A | HOH748 |
C | ASP288 |
C | ASP363 |
C | HOH571 |
C | HOH662 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue CA D 101 |
Chain | Residue |
C | ASP187 |
C | HOH505 |
D | GLU82 |
D | HOH209 |
D | HOH210 |
D | HOH212 |
site_id | AD1 |
Number of Residues | 10 |
Details | binding site for Di-peptide LEU D 71 and NLE D 72 |
Chain | Residue |
D | LEU67 |
D | HIS68 |
D | SER69 |
D | ALA70 |
D | GLU73 |
D | ALA74 |
D | ILE75 |
D | HIS76 |
C | THR351 |
C | MET355 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for Di-peptide NLE D 72 and GLU D 73 |
Chain | Residue |
D | HIS68 |
D | SER69 |
D | ALA70 |
D | LEU71 |
D | ALA74 |
D | ILE75 |
D | HIS76 |
D | SER77 |
D | HOH201 |
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 | 4 |
Details | MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134 |
Chain | Residue | Details |
A | MET44 | |
A | MET47 | |
C | MET44 | |
C | MET47 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS61 | |
C | LYS61 |
site_id | SWS_FT_FI3 |
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 | |
C | HIS73 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
Chain | Residue | Details |
A | LYS84 | |
C | LYS84 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 |
Chain | Residue | Details |
A | ARG177 | |
C | ARG177 |