Research workbench
Inhibition of leishmania major pteridine reductase (PTR1) by 2,4,6-triaminoquinazoline; structure of the NADP ternary complex.
Analyse Inhibition of leishmania major pteridine reductase (PTR1) by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W0C
- Type
- protein
- Length
- 2,130 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pteridine reductase
- EC
- 1.5.1.33
- UniProt
- Q01782
- Ligands
- TAQ, NAP
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 8 distinct chains · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pteridine reductase (EC 1.5.1.33) | protein | 276 | 45% helix, 15% strand | Q01782 |
| B | Pteridine reductase (EC 1.5.1.33) | protein | 274 | 46% helix, 16% strand | Q01782 |
| C | Pteridine reductase (EC 1.5.1.33) | protein | 264 | 46% helix, 15% strand | Q01782 |
| D | Pteridine reductase (EC 1.5.1.33) | protein | 256 | 46% helix, 15% strand | Q01782 |
| E | Pteridine reductase (EC 1.5.1.33) | protein | 267 | 48% helix, 15% strand | Q01782 |
| F | Pteridine reductase (EC 1.5.1.33) | protein | 270 | 47% helix, 16% strand | Q01782 |
| G | Pteridine reductase (EC 1.5.1.33) | protein | 263 | 46% helix, 14% strand | Q01782 |
| H | Pteridine reductase (EC 1.5.1.33) | protein | 260 | 44% helix, 16% strand | Q01782 |
Ligands and binding sites
- TAQ · 2,4,6-triaminoquinazoline · ligand · 9 copies · chains A, B, C, D, E, F, G, H
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1096 | 0.82 | 0.84 | 71 | empty |
| 2 | 1167 | 0.82 | 0.84 | 83 | empty |
| 3 | 735 | 0.73 | 0.79 | 64 | NAP, TAQ |
| 4 | 620 | 0.73 | 0.80 | 51 | NAP, TAQ |
| 5 | 618 | 0.73 | 0.80 | 50 | NAP, TAQ |
Interfaces
14 interfaces between chains.
- E–F · 2039 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 2002 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1931 Ų buried · 16 hydrogen bonds · protein-protein
- G–H · 1908 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 1632 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1W0C · Inhibition of Leishmania major pteridine reductase (PTR1) by 2,4,6-triaminoquinazoline… · the same entry in another collection · chain G against G, TM-score 1.00
- Q01782 · AlphaFold monomer V2.0 prediction for pteridine reductase 1 (Q01782) · a predicted model of the same protein · chain D 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 Q01782
- Elsewhere: RCSB PDB 1W0C · PDBe 1W0C · UniProt Q01782
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.