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X-ray crystal structure analysis of the catalytic domain of the oncogene product P21H-RAS complexed with caged GTP and mant dgppnhp

Analyse X-ray crystal structure analysis of the catalytic domain of the oncogene… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GNR
Type: protein
Length: 166 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.85
Source: Homo sapiens
Molecule: C-H-RAS P21 protein
UniProt: P01112
Ligands: CAG, MG
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · resolution 1.85 · 1 distinct chain · 36% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	C-H-RAS P21 protein	protein	166	36% helix, 26% strand	P01112

Ligands and binding sites

CAG · Guanosine 5'-triphosphate P3-[1-(2-nitrophenyl)ethyl ester] · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	122	0.43	0.77	26	MG, CAG

Compared structures

1GNR · X-ray crystal structure analysis of the catalytic domain of the oncogene product P21H-RAS… · the same entry in another collection · chain A against A, TM-score 1.00
P01112 · AlphaFold monomer V2.0 prediction for GTPase HRAS (P01112) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P01112
Elsewhere: RCSB PDB 1GNR · PDBe 1GNR · UniProt P01112

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