1LCU
Polylysine Induces an Antiparallel Actin Dimer that Nucleates Filament Assembly: Crystal Structure at 3.5 A Resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 412 |
| Chain | Residue |
| A | GLN147 |
| A | ASP164 |
| A | ATP390 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1412 |
| Chain | Residue |
| B | HOH5 |
| B | HOH11 |
| B | HOH21 |
| B | GLN1147 |
| B | ASP1164 |
| B | ATP1390 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 503 |
| Chain | Residue |
| A | TYR179 |
| A | ALA180 |
| B | GLN1364 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 506 |
| Chain | Residue |
| A | ARG193 |
| A | ARG216 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 507 |
| Chain | Residue |
| B | ARG1216 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CA A 508 |
| Chain | Residue |
| A | VAL40 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 512 |
| Chain | Residue |
| A | ARG157 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP A 390 |
| Chain | Residue |
| A | GLY23 |
| A | SER24 |
| A | GLY25 |
| A | LEU26 |
| A | LYS28 |
| A | GLY166 |
| A | ASP167 |
| A | GLY168 |
| A | VAL169 |
| A | LYS223 |
| A | GLU224 |
| A | GLY312 |
| A | THR313 |
| A | MET315 |
| A | TYR316 |
| A | LYS346 |
| A | LAR411 |
| A | CA412 |
| A | HOH517 |
| A | HOH539 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LAR A 411 |
| Chain | Residue |
| A | LEU26 |
| A | ILE44 |
| A | GLN69 |
| A | TYR79 |
| A | ASP167 |
| A | GLY192 |
| A | ARG193 |
| A | THR196 |
| A | GLU217 |
| A | ARG220 |
| A | LYS223 |
| A | ATP390 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP B 1390 |
| Chain | Residue |
| B | HOH5 |
| B | HOH11 |
| B | HOH21 |
| B | GLY1023 |
| B | SER1024 |
| B | GLY1025 |
| B | LEU1026 |
| B | LYS1028 |
| B | GLY1166 |
| B | ASP1167 |
| B | GLY1168 |
| B | VAL1169 |
| B | LYS1223 |
| B | GLU1224 |
| B | GLY1311 |
| B | GLY1312 |
| B | THR1313 |
| B | MET1315 |
| B | LAR1411 |
| B | CA1412 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LAR B 1411 |
| Chain | Residue |
| B | GLY1025 |
| B | LEU1026 |
| B | PRO1042 |
| B | GLN1069 |
| B | TYR1079 |
| B | ASP1167 |
| B | GLY1192 |
| B | ARG1193 |
| B | THR1196 |
| B | GLU1217 |
| B | ARG1220 |
| B | ATP1390 |
Functional Information from PROSITE/UniProt
| site_id | PS00406 |
| Number of Residues | 11 |
| Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
| Chain | Residue | Details |
| A | TYR63-GLY73 |
| site_id | PS00432 |
| Number of Residues | 9 |
| Details | ACTINS_2 Actins signature 2. WITKqEYDE |
| Chain | Residue | Details |
| A | TRP366-GLU374 |
| site_id | PS01132 |
| Number of Residues | 13 |
| Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
| Chain | Residue | Details |
| A | LEU114-ARG126 |
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 | MET54 | |
| A | MET57 | |
| B | MET1054 | |
| B | MET1057 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS71 | |
| B | LYS1071 |
| 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 | HIS83 | |
| B | HIS1083 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
| Chain | Residue | Details |
| A | LYS94 | |
| B | LYS1094 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 |
| Chain | Residue | Details |
| A | ARG187 | |
| B | ARG1187 |
