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Crystal structure of a putative sugar isomerase (LMO2234) from listeria monocytogenes at 1.70 a resolution

Analyse Crystal structure of a putative sugar isomerase (LMO2234) from listeria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2G0W
Type
protein
Length
560 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
LMO2234 protein
UniProt
Q4EPT5
Ligands
MG
Pockets
5 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALMO2234 proteinprotein27549% helix, 16% strandQ4EPT5
BLMO2234 proteinprotein28546% helix, 18% strandQ4EPT5

Ligands and binding sites

  • MG · Magnesium ion · metal · 4 copies · chains A, B
  • PG4 · Tetraethylene glycol · additive · chains B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11310.570.8323empty
2910.540.8421empty
31080.510.8219empty
41880.450.7419empty
5500.290.7513empty

Interfaces

1 interface between chains.

  • A–B · 124 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

  • 2G0W · Crystal structure of a putative sugar isomerase (LMO2234) from listeria monocytogenes at… · the same entry in another collection · chain A against A, TM-score 1.00

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