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Crystal structure of L-threonine transaldolase from pseudomonas fluorescens in internal aldimine state

Analyse Crystal structure of L-threonine transaldolase from pseudomonas fluorescens in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7K34
Type
protein
Length
1,764 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Threonine aldolase
EC
4.1.2.5
UniProt
A0A1X9LWZ7
Ligands
SO4
Pockets
8 · best druggability 0.85

Structure

x-ray diffraction · 3 distinct chains · 49% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AThreonine aldolase (EC 4.1.2.5)protein44049% helix, 13% strandA0A1X9LWZ7
B, DThreonine aldolase (EC 4.1.2.5)protein44149% helix, 13% strandA0A1X9LWZ7
CThreonine aldolase (EC 4.1.2.5)protein44250% helix, 13% strandA0A1X9LWZ7

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 9 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19030.850.8789SO4
25450.700.8046SO4
35410.700.7941SO4
4500.680.9616empty
55130.670.7840SO4

Interfaces

5 interfaces between chains.

  • A–B · 5229 Ų buried · 63 hydrogen bonds · protein-protein
  • C–D · 5148 Ų buried · 65 hydrogen bonds · protein-protein
  • B–D · 558 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 286 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 92 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (cofactor).

Compared structures

  • 7K34 · Crystal structure of L-threonine transaldolase from Pseudomonas fluorescens in internal… · the same entry in another collection · chain A against A, TM-score 1.00

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