Research workbench
Wild-type staphylococcus aureus DHFR in complex with trimethoprim
Analyse Wild-type staphylococcus aureus DHFR in complex with trimethoprim in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W9H
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- P0A017
- Ligands
- TOP
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase (EC 1.5.1.3) | protein | 157 | 20% helix, 36% strand | P0A017 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 314 | 0.66 | 0.81 | 40 | TOP |
Compared structures
- 2W9H · Wild-type Staphylococcus aureus DHFR in complex with trimethoprim · the same entry in another collection · chain A against A, TM-score 1.00
- P0A017 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P0A017) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P0A017
- Elsewhere: RCSB PDB 2W9H · PDBe 2W9H · UniProt P0A017
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