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Crystal structure of T. thermophilus methylenetetrahydrofolate dehydrogenase (mthfd)

Analyse Crystal structure of T. thermophilus methylenetetrahydrofolate dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6V6Y
Type
protein
Length
277 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bifunctional protein fold
EC
1.5.1.5, 3.5.4.9
UniProt
Q5SJ94
Ligands
NAP
Pockets
3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABifunctional protein fold (EC 1.5.1.5, 3.5.4.9)protein27744% helix, 18% strandQ5SJ94

Ligands and binding sites

  • NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14500.670.7848NAP
21650.450.7522empty
3550.330.7717empty

Compared structures

  • 6V6Y · Crystal Structure of T. thermophilus methylenetetrahydrofolate dehydrogenase (MTHFD) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5SJ94 · AlphaFold monomer V2.0 prediction for bifunctional protein fold (Q5SJ94) · a predicted model of the same protein · chain A against A, TM-score 0.98

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