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MolNFT v1 · #157257 · protein

A single reactive noncanonical amino acid is able to dramatically stabilize protein structure

6MTG · Homoserine O-succinyltransferase: “A single reactive noncanonical amino acid is able to dramatically stabilize protein structure”. X-ray diffraction, 9 pockets (best druggability 0.67). MolNFT v1 #157257 on GenesisL1: 3D structure…

PDB
6MTG
Type
protein
Length
583 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Homoserine O-succinyltransferase
EC
2.3.1.46
UniProt
P07623
Pockets
9 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHomoserine O-succinyltransferase (EC 2.3.1.46)protein29133% helix, 25% strandP07623
BHomoserine O-succinyltransferase (EC 2.3.1.46)protein29232% helix, 25% strandP07623

Ligands and binding sites

  • FMT · Formic acid · additive · 5 copies · chains A, B
  • PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
  • GOL · Glycerol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13170.670.8247empty
21870.650.8527PEG
31760.640.8529empty
42410.600.8026FMT
51640.560.8123empty

Interfaces

1 interface between chains.

  • A–B · 2236 Ų buried · 35 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

  • 6MTG · A Single Reactive Noncanonical Amino Acid is Able to Dramatically Stabilize Protein… · the same entry in another collection · chain A against A, TM-score 1.00
  • P07623 · AlphaFold monomer V2.0 prediction for homoserine O-succinyltransferase (P07623) · a predicted model of the same protein · chain A against A, TM-score 0.89

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