5MVV
Crystal structure of Plasmodium falciparum actin I- gelsolin segment 1 -CdATP complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005200 | molecular_function | structural constituent of cytoskeleton |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005884 | cellular_component | actin filament |
| A | 0007010 | biological_process | cytoskeleton organization |
| A | 0009665 | biological_process | plastid inheritance |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0020014 | biological_process | schizogony |
| A | 0070360 | biological_process | symbiont-mediated actin polymerization-dependent cell-to-cell migration in host |
| A | 0085017 | biological_process | entry into host cell by a symbiont-containing vacuole |
| G | 0051015 | molecular_function | actin filament binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | binding site for residue ATP A 401 |
| Chain | Residue |
| A | GLY14 |
| A | GLY183 |
| A | ARG211 |
| A | LYS214 |
| A | GLU215 |
| A | GLY302 |
| A | GLY303 |
| A | THR304 |
| A | MET306 |
| A | TYR307 |
| A | LYS337 |
| A | SER15 |
| A | CD403 |
| A | CD405 |
| A | HOH517 |
| A | HOH543 |
| A | HOH544 |
| A | HOH547 |
| A | HOH552 |
| A | HOH567 |
| A | HOH579 |
| A | HOH597 |
| A | GLY16 |
| A | ASN17 |
| A | LYS19 |
| A | GLY157 |
| A | ASP158 |
| A | GLY159 |
| A | VAL160 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue SCN A 402 |
| Chain | Residue |
| A | SER145 |
| A | SER146 |
| A | PRO333 |
| A | GLU335 |
| A | SER339 |
| A | HOH511 |
| A | HOH631 |
| G | GLN95 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CD A 403 |
| Chain | Residue |
| A | ATP401 |
| A | HOH517 |
| A | HOH547 |
| A | HOH567 |
| A | HOH661 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CD A 404 |
| Chain | Residue |
| A | THR319 |
| A | THR320 |
| A | ALA322 |
| A | SER324 |
| A | HOH614 |
| A | HOH766 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CD A 405 |
| Chain | Residue |
| A | ASP155 |
| A | GLY157 |
| A | VAL160 |
| A | ATP401 |
| A | HOH569 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 406 |
| Chain | Residue |
| A | GLU168 |
| G | ASP109 |
| G | GLY114 |
| G | ALA116 |
| G | HOH367 |
| G | HOH385 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CA G 201 |
| Chain | Residue |
| G | GLY65 |
| G | ASP66 |
| G | GLU97 |
| G | VAL145 |
| G | HOH372 |
| G | HOH382 |
Functional Information from PROSITE/UniProt
| site_id | PS00406 |
| Number of Residues | 11 |
| Details | ACTINS_1 Actins signature 1. FVGDEAQt.KRG |
| Chain | Residue | Details |
| A | PHE54-GLY64 |
| site_id | PS00432 |
| Number of Residues | 9 |
| Details | ACTINS_2 Actins signature 2. WITKeEYDE |
| Chain | Residue | Details |
| A | TRP357-GLU365 |
| site_id | PS01132 |
| Number of Residues | 13 |
| Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkgNR |
| Chain | Residue | Details |
| A | LEU105-ARG117 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24743229, ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:31199804, ECO:0007744|PDB:4CBU, ECO:0007744|PDB:4CBW, ECO:0007744|PDB:4CBX, ECO:0007744|PDB:5MVV, ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E, ECO:0007744|PDB:6I4F, ECO:0007744|PDB:6I4G, ECO:0007744|PDB:6I4H, ECO:0007744|PDB:6I4I, ECO:0007744|PDB:6I4J, ECO:0007744|PDB:6I4K, ECO:0007744|PDB:6I4L, ECO:0007744|PDB:6I4M |
| Chain | Residue | Details |
| G | GLY65 | |
| G | ASP66 | |
| G | GLU97 | |
| G | VAL145 | |
| A | GLY303 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24743229, ECO:0000269|PubMed:31199804, ECO:0007744|PDB:4CBU, ECO:0007744|PDB:4CBW, ECO:0007744|PDB:4CBX, ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E, ECO:0007744|PDB:6I4F, ECO:0007744|PDB:6I4H, ECO:0007744|PDB:6I4I, ECO:0007744|PDB:6I4J, ECO:0007744|PDB:6I4K, ECO:0007744|PDB:6I4L, ECO:0007744|PDB:6I4M |
| Chain | Residue | Details |
| G | ASP109 | |
| G | GLY114 | |
| G | ALA116 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| G | LYS135 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06396 |
| Chain | Residue | Details |
| G | TYR59 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24743229, ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:28923924, ECO:0000269|PubMed:31199804, ECO:0007744|PDB:4CBU, ECO:0007744|PDB:5MVV, ECO:0007744|PDB:5OGW, ECO:0007744|PDB:6I4D |
| Chain | Residue | Details |
| A | VAL160 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24743229, ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:31199804, ECO:0007744|PDB:4CBU, ECO:0007744|PDB:5MVV, ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E |
| Chain | Residue | Details |
| A | GLU215 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | SITE: Not methylated => ECO:0000269|PubMed:31199804 |
| Chain | Residue | Details |
| A | HIS74 |
