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Structure of chorismate mutase (form I) from thermus thermophilus HB8

Analyse Structure of chorismate mutase (form I) from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2D8D
Type
protein
Length
163 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phospho-2-dehydro-3-deoxyheptonate ALDOLASE/CHORISMATE mutase
EC
5.4.99.5
UniProt
Q72LN8
Ligands
CL
Pockets
2 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhospho-2-dehydro-3-deoxyheptonate ALDOLASE/CHORISMATE mutase (EC 5.4.99.5)protein8081% helix, 0% strandQ72LN8
BPhospho-2-dehydro-3-deoxyheptonate ALDOLASE/CHORISMATE mutase (EC 5.4.99.5)protein8383% helix, 0% strandQ72LN8

Ligands and binding sites

  • CL · Chloride ion · ion · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1880.720.9515empty
21380.650.8718CL

Interfaces

1 interface between chains.

  • A–B · 2591 Ų buried · 24 hydrogen bonds · protein-protein

Compared structures

  • 2D8D · Structure of Chorismate Mutase (Form I) from Thermus Thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00

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