4CBW
Crystal structure of Plasmodium berghei actin I with D-loop from muscle actin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| G | 0051015 | molecular_function | actin filament binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1377 |
| Chain | Residue |
| A | ATP1379 |
| A | HOH2003 |
| A | HOH2005 |
| A | HOH2006 |
| A | HOH2015 |
| A | HOH2022 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA G 1150 |
| Chain | Residue |
| G | ASP109 |
| G | GLY114 |
| G | ALA116 |
| A | GLU168 |
| A | HOH2024 |
| A | HOH2025 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA G 1151 |
| Chain | Residue |
| G | GLY65 |
| G | ASP66 |
| G | GLU97 |
| G | VAL145 |
| G | HOH2006 |
| G | HOH2015 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DIO A 1378 |
| Chain | Residue |
| A | TYR144 |
| A | TYR170 |
| A | PHE376 |
| G | GLN107 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP A 1379 |
| Chain | Residue |
| A | GLY14 |
| A | SER15 |
| A | GLY16 |
| A | ASN17 |
| A | LYS19 |
| A | GLY157 |
| A | ASP158 |
| A | GLY159 |
| A | VAL160 |
| A | GLY183 |
| A | LYS214 |
| A | GLU215 |
| A | GLY303 |
| A | THR304 |
| A | MET306 |
| A | CA1377 |
| A | HOH2006 |
| A | HOH2007 |
| A | HOH2021 |
| A | HOH2022 |
Functional Information from PROSITE/UniProt
| site_id | PS00406 |
| Number of Residues | 11 |
| Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
| Chain | Residue | Details |
| A | TYR54-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 | |
| A | GLY303 | |
| G | ASP66 | |
| G | GLU97 | |
| G | VAL145 | |
| A | ASP158 | |
| A | GLY159 | |
| A | VAL160 | |
| A | LYS214 | |
| A | GLU215 |
| 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 |
