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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: 1GNP
Type: protein
Length: 166 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-H-RAS P21 protein
UniProt: P01112
Ligands: AGN, MG
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	C-H-RAS P21 protein	protein	166	36% helix, 27% strand	P01112

Ligands and binding sites

AGN · Phosphoaminophosphonic acid 3'-O-(N-methylanthraniloyl-2'-deoxyguanylate 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	191	0.48	0.76	31	AGN

Compared structures

1GNP · 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

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 1GNP · PDBe 1GNP · UniProt P01112

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