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Refined crystal structure of the triphosphate conformation of H-RAS P21 at 1.35 ångströms resolution: implications for the mechanism of GTP hydrolysis

Analyse Refined crystal structure of the triphosphate conformation of H-RAS P21 at 1.35… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5P21
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 0.51

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

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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	219	0.51	0.76	31	MG, GNP

Compared structures

5P21 · Refined crystal structure of the triphosphate conformation of H-RAS P21 at 1.35 ångströms… · 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 5P21 · PDBe 5P21 · UniProt P01112

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