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Structure of MreB3 from Spiroplasma eriocheiris

Analyse Structure of MreB3 from Spiroplasma eriocheiris in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7E1G
Type
protein
Length
662 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.75
Source
Spiroplasma eriocheiris
Molecule
Cell shape-determining protein MreB
UniProt
A0A0H3XJK5
Ligands
ANP, MG
Pockets
6 · best druggability 0.74

Structure

x-ray diffraction · resolution 1.75 · 2 distinct chains · 40% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACell shape-determining protein MreBprotein33240% helix, 28% strandA0A0H3XJK5
BCell shape-determining protein MreBprotein33039% helix, 28% strandA0A0H3XJK5

Ligands and binding sites

  • ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14670.740.8358MG, ANP
24580.720.8258MG, ANP
34200.580.7438empty
4840.410.7815empty
5700.380.7814empty

Interfaces

1 interface between chains.

  • A–B · 230 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 42 modified, 1 covalent (methylation, covalent ligand).

Compared structures

  • 7E1G · Structure of MREB3 from spiroplasma eriocheiris · the same entry in another collection · chain A against A, TM-score 1.00

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