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GRB2 SH2 domain in phosphopeptide free form

Analyse GRB2 SH2 domain in phosphopeptide free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ICG
Type
protein
Length
190 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Growth factor receptor-bound protein 2
UniProt
P62993
Ligands
SO4
Pockets
2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGrowth factor receptor-bound protein 2protein9518% helix, 29% strandP62993

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 5 copies · chains A, B
  • GOL · Glycerol · additive · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11570.660.8739SO4
21020.480.8019empty

Interfaces

1 interface between chains.

  • A–B · 845 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 6ICG · Grb2 SH2 domain in phosphopeptide free form · the same entry in another collection · chain A against A, TM-score 1.00

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