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Crystal structure of the FAD-containing fnr-like module of human methionine synthase reductase

Analyse Crystal structure of the FAD-containing fnr-like module of human methionine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2QTL
Type
protein
Length
448 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methionine synthase reductase
EC
1.16.1.8
UniProt
Q9UBK8
Ligands
FAD
Pockets
3 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMethionine synthase reductase (EC 1.16.1.8)protein44834% helix, 21% strandQ9UBK8

Ligands and binding sites

  • FAD · Flavin-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
11990.570.8033empty
22480.510.7530FAD
31380.430.7629empty

Modifications

Observed in the structure: 3 modified (oxidation).

Compared structures

  • 2QTL · Crystal Structure of the FAD-containing FNR-like Module of Human Methionine Synthase… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UBK8 · AlphaFold monomer V2.0 prediction for methionine synthase reductase (Q9UBK8) · a predicted model of the same protein · chain A against A, TM-score 0.98

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