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Crystal structure of S-adenosylmethionine decarboxylase from potato

Analyse Crystal structure of S-adenosylmethionine decarboxylase from potato in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1MHM
Type
protein
Length
307 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
S-adenosylmethionine decarboxylase
EC
4.1.1.50
UniProt
Q04694
Ligands
PYR
Pockets
3 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BS-adenosylmethionine decarboxylase (EC 4.1.1.50)protein5426% helix, 39% strandQ04694
AS-adenosylmethionine decarboxylase (EC 4.1.1.50)protein25326% helix, 39% strandQ04694

Ligands and binding sites

  • PYR · Pyruvic acid · ligand · chains B, 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
13470.640.7940empty
21520.500.7921PYR
3850.480.8228empty

Interfaces

1 interface between chains.

  • B–A · 2650 Ų buried · 41 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 1MHM · Crystal structure of S-adenosylmethionine decarboxylase from potato · the same entry in another collection · chain B against B, TM-score 1.00
  • Q04694 · AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme… · a predicted model of the same protein · chain A against A, TM-score 0.99

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