MolNFT v1 · #17745 · protein

H-RAS 166 in aqueous mother liqour, rt

1P2T · Transforming protein P21/H-RAS-1: “H-RAS 166 in aqueous mother liqour, rt”. X-ray diffraction, 2 ligands (GNP, MG), 1 pocket (best druggability 0.49). MolNFT v1 #17745 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1P2T
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transforming protein P21/H-RAS-1
UniProt: P01112
Ligands: GNP, MG
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transforming protein P21/H-RAS-1	protein	162	36% 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	191	0.49	0.76	30	MG, GNP

Compared structures

1P2T · H-Ras 166 in Aqueous mother liqour, RT · 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 1P2T · PDBe 1P2T · UniProt P01112

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