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N-terminal SH2 domain of the P120RASGAP bound to a P190RHOGAP phosphotyrosine peptide

Analyse N-terminal SH2 domain of the P120RASGAP bound to a P190RHOGAP phosphotyrosine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PXC
Type
protein
Length
116 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RAS GTPase-activating protein 1; Phosphopeptide of P190RHOGAP
UniProt
P20936
Ligands
ACE

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARAS GTPase-activating protein 1protein10424% helix, 37% strandP20936
UPhosphopeptide of P190RHOGAPprotein120% helix, 8% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains U

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

Interfaces

1 interface between chains.

  • A–U · 686 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 modified (covalent ligand, phosphorylation).

Compared structures

  • 6PXC · N-Terminal SH2 domain of the p120RasGAP bound to a p190RhoGAP phosphotyrosine peptide · the same entry in another collection · chain U against U, TM-score 1.00
  • P20936 · AlphaFold monomer V2.0 prediction for RAS GTPase-activating protein 1 (P20936) · a predicted model of the same protein · chain A against A, TM-score 0.96

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