Research workbench
Staphylococcus aureus F98Y dihydrofolate reductase mutant complexed with beta-NADPH and 3'-(3-(2,4-diamino-6-ethylpyrimidin-5-YL)PROP-2- yn-1-yl)-4'-methoxy-[1,1'-biphenyl]-4-carboxylic acid (UCP1106)
Analyse Staphylococcus aureus F98Y dihydrofolate reductase mutant complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ISP
- 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
- NAP, U06
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Dihydrofolate reductase (EC 1.5.1.3) | protein | 157 | 20% helix, 34% strand | P0A017 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains X
- U06 · 4-[3-[3-[2,4-bis(azanyl)-6-ethyl-pyrimidin-5-yl]prop-2-ynyl]-4-methoxy-phenyl]benzoic acid · ligand · chains X
- GOL · Glycerol · additive · chains X
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 | 334 | 0.68 | 0.82 | 39 | NAP, U06 |
Compared structures
- 5ISP · Staphylococcus aureus F98Y Dihydrofolate Reductase mutant complexed with beta-NADPH and… · the same entry in another collection · chain X against X, TM-score 1.00
- P0A017 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P0A017) · a predicted model of the same protein · chain X 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 5ISP · PDBe 5ISP · UniProt P0A017
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