4Y6P
Structure of Plasmodium falciparum DXR in complex with a beta-substituted fosmidomycin analogue, RC177, 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 | 19 |
| Details | binding site for residue R77 A 501 |
| Chain | Residue |
| A | LYS205 |
| A | ASN311 |
| A | LYS312 |
| A | GLU315 |
| A | PRO358 |
| A | ASP359 |
| A | MN502 |
| A | HOH671 |
| A | HOH683 |
| A | HOH811 |
| A | HOH835 |
| A | ASP231 |
| A | SER232 |
| A | GLU233 |
| A | SER269 |
| A | SER270 |
| A | HIS293 |
| A | TRP296 |
| A | SER306 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 502 |
| Chain | Residue |
| A | LYS205 |
| A | ASP231 |
| A | GLU233 |
| A | GLU315 |
| A | R77501 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue R77 B 501 |
| Chain | Residue |
| B | LYS205 |
| B | ASP231 |
| B | SER232 |
| B | GLU233 |
| B | SER269 |
| B | SER270 |
| B | SER306 |
| B | ASN311 |
| B | LYS312 |
| B | GLU315 |
| B | HIS341 |
| B | PRO358 |
| B | ASP359 |
| B | MN502 |
| B | HOH682 |
| B | HOH688 |
| B | HOH853 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 502 |
| Chain | Residue |
| B | LYS205 |
| B | ASP231 |
| B | GLU233 |
| B | GLU315 |
| B | R77501 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 503 |
| Chain | Residue |
| A | ASP242 |
| A | HOH691 |
| A | HOH714 |
| B | GLN239 |
| B | LEU241 |
| B | HOH728 |
| B | HOH737 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| B | THR91 |
| B | LEU94 |
| B | ASN95 |
| B | ARG98 |
| B | GLN124 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O96693","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P45568","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25781377","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27487410","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Y67","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y6P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y6R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5JAZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5JBI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5JC1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5JMP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5JMW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5JNL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5JO0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
