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Crystal structures of D-allulose 3-epimerase with D-sorbose from sinorhizobium fredii

Analyse Crystal structures of D-allulose 3-epimerase with D-sorbose from sinorhizobium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DZ5
Type
protein
Length
1,130 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
D-tagatose 3-epimerase
UniProt
A0A249Q1V1
Ligands
SDD, HVC, MG
Pockets
10 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CD-tagatose 3-epimeraseprotein28345% helix, 15% strandA0A249Q1V1
B, DD-tagatose 3-epimeraseprotein28245% helix, 15% strandA0A249Q1V1

Ligands and binding sites

  • SDD · D-sorbose · ligand · 4 copies · chains A, B, C, D
  • HVC · alpha-D-Sorbopyranose · ligand · 3 copies · chains A, C, D
  • MG · Magnesium ion · metal · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16120.870.9357empty
2740.750.9823SDD
3710.740.9823SDD
43110.690.8345SDD
52600.690.8434SDD

Interfaces

6 interfaces between chains.

  • B–C · 1642 Ų buried · 28 hydrogen bonds · protein-protein
  • A–D · 1635 Ų buried · 27 hydrogen bonds · protein-protein
  • A–B · 571 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 567 Ų buried · 11 hydrogen bonds · protein-protein
  • B–D · 423 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 7DZ5 · Crystal structures of D-allulose 3-epimerase with D-sorbose from Sinorhizobium fredii · the same entry in another collection · chain A against A, TM-score 1.00

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