MolNFT v1 · #5105 · protein
One active site, two modes of reduction correlate the mechanism of leishmania pteridine reductase with pterin metabolism and antifolate drug resistance in trpanosomes
1E7W: “One active site, two modes of reduction correlate the mechanism of leishmania pteridine reductase with pterin…”. X-ray diffraction, 2 ligands (NDP, MTX), 5 pockets (best druggability 0.73). MolNFT v1 #5105 on GenesisL1: 3D…
- PDB
- 1E7W
- Type
- protein
- Length
- 525 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pteridine reductase
- EC
- 1.1.1.253
- UniProt
- Q9U1F8
- Ligands
- NDP, MTX
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pteridine reductase (EC 1.1.1.253) | protein | 267 | 48% helix, 15% strand | Q9U1F8 |
| B | Pteridine reductase (EC 1.1.1.253) | protein | 258 | 48% helix, 17% strand | Q9U1F8 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- MTX · Methotrexate · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 599 | 0.73 | 0.80 | 48 | NDP, MTX, EDO |
| 2 | 587 | 0.72 | 0.80 | 48 | NDP, MTX, EDO |
| 3 | 234 | 0.58 | 0.79 | 31 | empty |
| 4 | 69 | 0.35 | 0.78 | 22 | EDO |
| 5 | 50 | 0.26 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1898 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1E7W · One active site, two modes of reduction correlate the mechanism of leishmania pteridine… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9U1F8
- Elsewhere: RCSB PDB 1E7W · PDBe 1E7W · UniProt Q9U1F8
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