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Mutant DNA polymerase sliding clamp from escherichia COLI with bound P7 peptide

Analyse Mutant DNA polymerase sliding clamp from escherichia COLI with bound P7 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6FVM
Type
protein
Length
746 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta sliding clamp; P7 peptide
UniProt
P0A990
Ligands
ACE, CA
Pockets
11 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BBeta sliding clampprotein36822% helix, 47% strandP0A990
H, IP7 peptideprotein50% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · 2 copies · chains A, H, B, I
  • CA · Calcium ion · metal · chains A
  • 1PE · Pentaethylene glycol · additive · 9 copies · chains A, B
  • GOL · Glycerol · additive · chains A

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

Pockets

11 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1870.410.7817empty
2680.360.7714empty
3560.350.7915empty
4610.340.7719empty
5890.340.74221PE

Interfaces

3 interfaces between chains.

  • A–B · 1307 Ų buried · 31 hydrogen bonds · protein-protein
  • A–H · 549 Ų buried · 5 hydrogen bonds · protein-protein
  • B–I · 547 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent, 2 modified (covalent ligand, nonstandard).

Compared structures

  • 6FVM · Mutant DNA polymerase sliding clamp from Escherichia coli with bound P7 peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A990 · AlphaFold monomer V2.0 prediction for beta sliding clamp (P0A990) · a predicted model of the same protein · chain B against A, TM-score 0.98

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