4Y6S
Structure of Plasmodium falciparum DXR in complex with a beta-substituted fosmidomycin analogue, RC134, and manganese
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 501 |
| Chain | Residue |
| A | LYS205 |
| A | ASP231 |
| A | GLU233 |
| A | GLU315 |
| A | 48S502 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue 48S A 502 |
| Chain | Residue |
| A | SER270 |
| A | TRP296 |
| A | MET298 |
| A | SER306 |
| A | ASN311 |
| A | LYS312 |
| A | GLU315 |
| A | MN501 |
| A | HOH647 |
| A | HOH725 |
| A | HOH742 |
| A | ASP231 |
| A | SER232 |
| A | GLU233 |
| A | SER269 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 501 |
| Chain | Residue |
| B | LYS205 |
| B | ASP231 |
| B | GLU233 |
| B | GLU315 |
| B | 48S502 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue 48S B 502 |
| Chain | Residue |
| B | LYS205 |
| B | ASP231 |
| B | SER232 |
| B | GLU233 |
| B | SER269 |
| B | SER270 |
| B | TRP296 |
| B | MET298 |
| B | ILE302 |
| B | SER306 |
| B | ASN311 |
| B | LYS312 |
| B | GLU315 |
| B | MN501 |
| B | HOH674 |
| B | HOH706 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O96693 |
| Chain | Residue | Details |
| A | THR86 | |
| A | ASN115 | |
| A | GLU206 | |
| A | GLY299 | |
| B | THR86 | |
| B | ASN115 | |
| B | GLU206 | |
| B | GLY299 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P45568 |
| Chain | Residue | Details |
| A | LYS205 | |
| B | SER270 | |
| B | HIS293 | |
| B | SER306 | |
| B | ASN311 | |
| B | LYS312 | |
| A | SER232 | |
| A | SER270 | |
| A | HIS293 | |
| A | SER306 | |
| A | ASN311 | |
| A | LYS312 | |
| B | LYS205 | |
| B | SER232 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25781377, ECO:0000269|PubMed:27487410, ECO:0007744|PDB:4Y67, ECO:0007744|PDB:4Y6P, ECO:0007744|PDB:4Y6R, ECO:0007744|PDB:4Y6S, ECO:0007744|PDB:5JAZ, ECO:0007744|PDB:5JBI, ECO:0007744|PDB:5JC1, ECO:0007744|PDB:5JMP, ECO:0007744|PDB:5JMW, ECO:0007744|PDB:5JNL, ECO:0007744|PDB:5JO0 |
| Chain | Residue | Details |
| A | ASP231 | |
| A | GLU233 | |
| A | GLU315 | |
| B | ASP231 | |
| B | GLU233 | |
| B | GLU315 |
