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Crystal structure of the ternary mtx NADPH complex of escherichia COLI dihydrofolate reductase

Analyse Crystal structure of the ternary mtx NADPH complex of escherichia COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3DAU
Type
protein
Length
159 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dihydrofolate reductase
EC
1.5.1.3
UniProt
P0ABQ4
Ligands
MTX, NDP
Pockets
1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADihydrofolate reductase (EC 1.5.1.3)protein15925% helix, 34% strandP0ABQ4

Ligands and binding sites

  • MTX · Methotrexate · ligand · chains A
  • NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A

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
13390.660.8144MTX, NDP

Compared structures

  • 3DAU · Crystal structure of the ternary MTX NADPH complex of Escherichia coli dihydrofolate… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0ABQ4 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P0ABQ4) · a predicted model of the same protein · chain A against A, TM-score 0.99

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