MolNFT v1 · #191135 · protein

Three-dimensional structures and properties of a transforming and a nontransforming glycine-12 mutant of P21H-RAS

821P · C-H-RAS P21 protein: “Three-dimensional structures and properties of a transforming and a nontransforming glycine-12 mutant of…”. X-ray diffraction, 2 ligands (GNP, MG), 1 pocket (best druggability 0.50). MolNFT v1 #191135 on…

PDB: 821P
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: GNP, MG
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	C-H-RAS P21 protein	protein	166	37% helix, 28% strand	P01112

Ligands and binding sites

GNP · Phosphoaminophosphonic acid-guanylate 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	205	0.50	0.76	32	MG, GNP

Compared structures

821P · Three-dimensional structures and properties of a transforming and a nontransforming… · 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 821P · PDBe 821P · UniProt P01112

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