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S. aureus Dihydrofolate Reductase complexed with novel 7-aryl-2,4-diaminoquinazolines

Analyse S. aureus Dihydrofolate Reductase complexed with novel… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3SRS
Type
protein
Length
157 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.7
Source
Staphylococcus aureus
Molecule
Dihydrofolate reductase
EC
1.5.1.3
UniProt
P0A017
Ligands
M23, NAP
Pockets
1 · best druggability 0.70

Structure

x-ray diffraction · resolution 1.7 · 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

  • M23 · 7-(5-bromo-2-ethoxyphenyl)-6-methylquinazoline-2,4-diamine · ligand · chains X
  • NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · 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
13290.700.8337M23, NAP

Compared structures

  • 3SRS · 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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