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S. aureus dihydrofolate reductase complexed with novel 7-aryl-2,4- diaminoquinazolines

Analyse S. aureus dihydrofolate reductase complexed with novel 7-aryl-2,4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3SRQ
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, Q19
Pockets
1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
XDihydrofolate reductase (EC 1.5.1.3)protein15720% helix, 36% strandP0A017

Ligands and binding sites

  • NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains X
  • Q19 · 1-[3-(2,4-diamino-6-methylquinazolin-7-yl)phenyl]ethanone · ligand · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13620.660.8040NAP, Q19

Compared structures

  • 3SRQ · S. aureus Dihydrofolate Reductase complexed with novel 7-aryl-2,4-diaminoquinazolines · 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

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