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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 v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.6
Source: Homo sapiens; SYNTHETIC CONSTRUCT
Molecule: Ras GTPase-activating protein 1; phosphopeptide of p190RhoGAP
UniProt: P20936

Structure

x-ray diffraction · resolution 1.6 · 2 distinct chains · 22% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ras GTPase-activating protein 1	protein	104	24% helix, 37% strand	P20936
U	phosphopeptide of p190RhoGAP	protein	12	0% helix, 8% strand	—

Interfaces

1 interface between chains.

A–U · 686 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

6PXC · N-terminal SH2 domain of the P120RASGAP bound to a P190RHOGAP phosphotyrosine peptide · the same entry in another collection · chain A against A, 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

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P20936
Elsewhere: RCSB PDB 6PXC · PDBe 6PXC · UniProt P20936

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