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Bacteriophage lambda SER/THR protein phosphatase

Analyse Bacteriophage lambda SER/THR protein phosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1G5B
Type
protein
Length
661 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.15
Source
Enterobacteria phage lambda
Molecule
SERINE/THREONINE protein phosphatase
EC
3.1.3.-
UniProt
P03772
Ligands
MN, HG, SO4
Pockets
6 · best druggability 0.65

Structure

x-ray diffraction · resolution 2.15 · 2 distinct chains · 34% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASERINE/THREONINE protein phosphatase (EC 3.1.3.-)protein21934% helix, 20% strandP03772
B, CSERINE/THREONINE protein phosphatase (EC 3.1.3.-)protein22134% helix, 19% strandP03772

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 6 copies · chains A, B, C
  • HG · Mercury (II) ion · metal · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 4 copies · chains A, B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14080.650.7939MN, HG, SO4
21650.490.7724empty
3570.330.7711empty
4660.300.7418MN, SO4
5560.290.7512empty

Interfaces

2 interfaces between chains.

  • A–C · 511 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 338 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 1G5B · Bacteriophage lambda SER/THR protein phosphatase · the same entry in another collection · chain A against A, TM-score 1.00

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