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Nahe wt selenomethionine

Analyse Nahe wt selenomethionine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6DAO
Type
protein
Length
650 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Trans-O-hydroxybenzylidenepyruvate hydratase-aldolase
EC
4.1.2.45
UniProt
Q51947
Pockets
4 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BTrans-O-hydroxybenzylidenepyruvate hydratase-aldolase (EC 4.1.2.45)protein32450% helix, 12% strandQ51947
ATrans-O-hydroxybenzylidenepyruvate hydratase-aldolase (EC 4.1.2.45)protein32650% helix, 12% strandQ51947

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111560.770.7985empty
21950.550.7927empty
32080.540.7828empty
4720.320.7414empty

Interfaces

1 interface between chains.

  • B–A · 808 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 22 modified (engineered).

Compared structures

  • 6DAO · NahE WT selenomethionine · the same entry in another collection · chain B against B, TM-score 1.00
  • Q51947 · AlphaFold monomer V2.0 prediction for trans-O- hydroxybenzylidenepyruvate… · a predicted model of the same protein · chain B against A, TM-score 0.99

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