6I4L
Crystal Structure of Plasmodium falciparum actin I (G115A mutant) in the Mg-K-ATP/ADP state
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 | 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 | ADP402 |
| A | MG403 |
| A | HOH509 |
| A | HOH522 |
| A | HOH524 |
| A | HOH526 |
| A | HOH602 |
| A | HOH614 |
| A | HOH654 |
| A | HOH678 |
| A | GLY16 |
| A | ASN17 |
| A | LYS19 |
| A | GLY157 |
| A | ASP158 |
| A | GLY159 |
| A | VAL160 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | binding site for residue ADP A 402 |
| Chain | Residue |
| A | GLY14 |
| A | SER15 |
| A | GLY16 |
| A | ASN17 |
| A | LYS19 |
| A | GLY157 |
| A | ASP158 |
| A | GLY183 |
| A | ARG211 |
| A | LYS214 |
| A | GLU215 |
| A | GLY302 |
| A | GLY303 |
| A | THR304 |
| A | MET306 |
| A | TYR307 |
| A | LYS337 |
| A | ATP401 |
| A | MG403 |
| A | HOH522 |
| A | HOH524 |
| A | HOH526 |
| A | HOH556 |
| A | HOH602 |
| A | HOH650 |
| A | HOH678 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ATP401 |
| A | ADP402 |
| A | HOH522 |
| A | HOH541 |
| A | HOH556 |
| A | HOH650 |
| A | HOH678 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue SCN A 404 |
| Chain | Residue |
| A | VAL22 |
| A | HOH652 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA G 201 |
| Chain | Residue |
| G | GLY41 |
| G | ASP42 |
| G | GLU73 |
| G | VAL121 |
| G | HOH377 |
| G | HOH381 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA G 202 |
| Chain | Residue |
| A | GLU168 |
| G | ASP85 |
| G | GLY90 |
| G | ALA92 |
| G | HOH340 |
| G | HOH365 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue SCN G 203 |
| Chain | Residue |
| G | TYR116 |
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. LLTEApLNPkaNR |
| 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 |
| G | ARG91 | |
| G | ALA122 | |
| A | LYS214 | |
| A | GLY303 | |
| G | GLY90 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06396 |
| Chain | Residue | Details |
| G | LEU84 |
| 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 |
