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Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the product

Analyse Crystal structure of the human S-adenosylmethionine synthetase 1 in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2OBV
Type
protein
Length
384 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
S-adenosylmethionine synthetase isoform type-1
EC
2.5.1.6
UniProt
Q00266
Ligands
SAM, NA
Pockets
1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AS-adenosylmethionine synthetase isoform type-1 (EC 2.5.1.6)protein38434% helix, 26% strandQ00266

Ligands and binding sites

  • SAM · S-adenosylmethionine · ligand · chains A
  • NA · Sodium ion · metal · 2 copies · chains A
  • PG4 · Tetraethylene glycol · additive · 3 copies · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1600.330.7714empty

Compared structures

  • 2OBV · Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q00266 · AlphaFold monomer V2.0 prediction for S-adenosylmethionine synthase isoform type-1… · a predicted model of the same protein · chain A against A, TM-score 0.99

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