4O7M
Crystal structure of a trap periplasmic solute binding protein from shewanella loihica PV-4, target EFI-510273, with bound L-malate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0015740 | biological_process | C4-dicarboxylate transport |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0055085 | biological_process | transmembrane transport |
| B | 0015740 | biological_process | C4-dicarboxylate transport |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0055085 | biological_process | transmembrane transport |
| C | 0015740 | biological_process | C4-dicarboxylate transport |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0055085 | biological_process | transmembrane transport |
| D | 0015740 | biological_process | C4-dicarboxylate transport |
| D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LMR A 401 |
| Chain | Residue |
| A | VAL41 |
| A | ASN220 |
| A | TYR243 |
| A | HOH509 |
| A | HOH513 |
| A | VAL42 |
| A | LYS48 |
| A | SER98 |
| A | LYS101 |
| A | ARG176 |
| A | MSE178 |
| A | PHE199 |
| A | ASN216 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 401 |
| Chain | Residue |
| B | TYR227 |
| B | GLU228 |
| B | SER292 |
| B | ARG294 |
| B | HOH826 |
| B | HOH888 |
| B | HOH1075 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LMR B 402 |
| Chain | Residue |
| B | VAL41 |
| B | VAL42 |
| B | LYS48 |
| B | SER98 |
| B | LYS101 |
| B | ARG176 |
| B | MSE178 |
| B | PHE199 |
| B | ASN216 |
| B | ASN220 |
| B | TYR243 |
| B | HOH506 |
| B | HOH526 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LMR C 401 |
| Chain | Residue |
| C | VAL41 |
| C | VAL42 |
| C | LYS48 |
| C | SER98 |
| C | LYS101 |
| C | ARG176 |
| C | MSE178 |
| C | PHE199 |
| C | ASN216 |
| C | ASN220 |
| C | TYR243 |
| C | HOH503 |
| C | HOH507 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LMR D 401 |
| Chain | Residue |
| D | VAL41 |
| D | VAL42 |
| D | LYS48 |
| D | SER98 |
| D | LYS101 |
| D | ARG176 |
| D | MSE178 |
| D | PHE199 |
| D | ASN216 |
| D | ASN220 |
| D | TYR243 |
| D | HOH516 |
| D | HOH1014 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25540822, ECO:0007744|PDB:4OA4 |
| Chain | Residue | Details |
| A | LYS48 | |
| B | ASN216 | |
| B | ASN220 | |
| B | TYR243 | |
| C | LYS48 | |
| C | LYS101 | |
| C | ARG176 | |
| C | ASN216 | |
| C | ASN220 | |
| C | TYR243 | |
| D | LYS48 | |
| A | LYS101 | |
| D | LYS101 | |
| D | ARG176 | |
| D | ASN216 | |
| D | ASN220 | |
| D | TYR243 | |
| A | ARG176 | |
| A | ASN216 | |
| A | ASN220 | |
| A | TYR243 | |
| B | LYS48 | |
| B | LYS101 | |
| B | ARG176 |
