GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from saccharomyces cerevisiae complexed with NAD

Analyse Crystal structure of the NAD-dependent 5,10-methylenetetrahydrofolate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1EE9
Type
protein
Length
317 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
5,10-methylenetetrahydrofolate dehydrogenase
EC
1.5.1.15
UniProt
Q02046
Ligands
NAD
Pockets
3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A5,10-methylenetetrahydrofolate dehydrogenase (EC 1.5.1.15)protein31739% helix, 19% strandQ02046

Ligands and binding sites

  • NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14690.730.8242NAD
22080.530.7821empty
3610.330.7613empty

Compared structures

  • 1EE9 · Crystal structure of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q02046 · AlphaFold monomer V2.0 prediction for methylenetetrahydrofolate dehydrogenase [NAD(+)]… · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.