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Cryo-EM structure of the Gp168-beta-clamp complex

Analyse Cryo-EM structure of the Gp168-beta-clamp complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EVP
Type
protein
Length
840 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.2
Source
Staphylococcus aureus; Staphylococcus virus Twort
Molecule
Beta sliding clamp; Sliding clamp inhibitor
UniProt
P0A024, A0A6H0X5G8
Pockets
5 · best druggability 0.72

Structure

electron microscopy · resolution 3.2 · 2 distinct chains · 22% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BBeta sliding clampprotein37716% helix, 36% strandP0A024
C, DSliding clamp inhibitorprotein4377% helix, 0% strandA0A6H0X5G8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111380.720.7687empty
211090.720.7691empty
3610.330.7617empty
4540.320.7714empty
5560.290.7615empty

Interfaces

6 interfaces between chains.

  • A–B · 1256 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 843 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 527 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 524 Ų buried · 5 hydrogen bonds · protein-protein
  • C–B · 249 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 7EVP · Cryo-EM structure of the GP168-beta-clamp complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A024 · AlphaFold monomer V2.0 prediction for beta sliding clamp (P0A024) · a predicted model of the same protein · chain A against A, TM-score 0.97

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