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Crystal structure of homoserine O-succinyltransferase from escherichia COLI K-12

Analyse Crystal structure of homoserine O-succinyltransferase from escherichia COLI K-12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7CBE
Type
protein
Length
575 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
Ligands
SO4
Pockets
6 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHomoserine O-succinyltransferase (EC 2.3.1.46)protein28334% helix, 26% strandP07623
BHomoserine O-succinyltransferase (EC 2.3.1.46)protein29233% helix, 25% strandP07623

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · chains A, B
  • GOL · Glycerol · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11870.640.8527empty
22560.640.8139GOL
32360.630.8239empty
42160.630.8336EDO
52240.500.7634empty

Interfaces

1 interface between chains.

  • A–B · 2447 Ų buried · 44 hydrogen bonds · protein-protein

Compared structures

  • 7CBE · Crystal structure of Homoserine O-succinyltransferase from Escherichia coli K-12 · 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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