4CBU
Crystal structure of Plasmodium falciparum actin I
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 | 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 | 27 |
| Details | BINDING SITE FOR RESIDUE ATP A 1369 |
| 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 | CA1370 |
| A | HOH2006 |
| A | HOH2010 |
| A | HOH2016 |
| A | HOH2020 |
| A | HOH2085 |
| A | HOH2100 |
| A | HOH2592 |
| A | GLY16 |
| A | ASN17 |
| A | LYS19 |
| A | GLY157 |
| A | ASP158 |
| A | GLY159 |
| A | VAL160 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1370 |
| Chain | Residue |
| A | ATP1369 |
| A | HOH2005 |
| A | HOH2010 |
| A | HOH2016 |
| A | HOH2025 |
| A | HOH2027 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA G 1150 |
| Chain | Residue |
| G | GLY65 |
| G | ASP66 |
| G | GLU97 |
| G | VAL145 |
| G | HOH2007 |
| G | HOH2013 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA G 1151 |
| Chain | Residue |
| A | GLU168 |
| A | HOH2069 |
| A | HOH2102 |
| G | ASP109 |
| G | GLY114 |
| G | ALA116 |
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 | 3 |
| 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 |
| A | GLY303 | |
| A | LYS214 | |
| G | GLY114 | |
| G | ARG115 | |
| G | ALA146 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06396 |
| Chain | Residue | Details |
| G | LEU108 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24743229, ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:28923924, ECO:0000269|PubMed:31199804, ECO:0000269|PubMed:33767187, ECO:0000269|Ref.7, ECO:0007744|PDB:4CBU, ECO:0007744|PDB:5MVV, ECO:0007744|PDB:5OGW, ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E, ECO:0007744|PDB:6TU4, ECO:0007744|PDB:7ALN |
| Chain | Residue | Details |
| A | LYS19 |
| site_id | SWS_FT_FI4 |
| 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 |
| Chain | Residue | Details |
| A | GLY159 |
| 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 |
