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Structure of bacteriophage T4 endoii E118A mutant

Analyse Structure of bacteriophage T4 endoii E118A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2WSH
Type
protein
Length
527 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Endonuclease II
EC
3.1.21.-
UniProt
P07059
Ligands
PO4
Pockets
5 · best druggability 0.71

Structure

x-ray diffraction · 4 distinct chains · 33% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndonuclease II (EC 3.1.21.-)protein13432% helix, 32% strandP07059
BEndonuclease II (EC 3.1.21.-)protein13134% helix, 32% strandP07059
CEndonuclease II (EC 3.1.21.-)protein12934% helix, 33% strandP07059
DEndonuclease II (EC 3.1.21.-)protein13333% helix, 33% strandP07059

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains A
  • PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11780.710.8826empty
2940.700.9422empty
3910.360.7514empty
4500.290.7617empty
5550.240.7114empty

Interfaces

6 interfaces between chains.

  • C–D · 688 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 659 Ų buried · 8 hydrogen bonds · protein-protein
  • B–C · 532 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 394 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 379 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 2WSH · Structure of bacteriophage T4 EndoII E118A mutant · the same entry in another collection · chain A against A, TM-score 1.00

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