Research workbench
Structure of pteridine reductase 1 (PTR1) from trypanosoma brucei in ternary complex with cofactor (NADP+) and substrate (folate)
Analyse Structure of pteridine reductase 1 (PTR1) from trypanosoma brucei in ternary… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BMC
- Type
- protein
- Length
- 994 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pteridine reductase
- UniProt
- O76290
- Ligands
- NAP, FOL
- Pockets
- 7 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Pteridine reductase | protein | 249 | 49% helix, 15% strand | O76290 |
| B, C | Pteridine reductase | protein | 248 | 49% helix, 14% strand | O76290 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
- FOL · Folic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1195 | 0.84 | 0.85 | 69 | empty |
| 2 | 610 | 0.77 | 0.83 | 46 | NAP, FOL |
| 3 | 611 | 0.77 | 0.83 | 49 | NAP, FOL |
| 4 | 585 | 0.77 | 0.83 | 47 | NAP, FOL |
| 5 | 560 | 0.76 | 0.83 | 47 | NAP, FOL |
Interfaces
6 interfaces between chains.
- B–D · 1865 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 1830 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 1421 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1411 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 565 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 3BMC · Structure of Pteridine Reductase 1 (PTR1) from Trypanosoma brucei in ternary complex with… · the same entry in another collection · chain B against B, 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 O76290
- Elsewhere: RCSB PDB 3BMC · PDBe 3BMC · UniProt O76290
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.