MolNFT v1 · #176517 · protein

H-RAS Q61H in complex with gppnhp (state 1) after structural transition by humidity control

7DPH · GTPase HRAS: “H-RAS Q61H in complex with gppnhp (state 1) after structural transition by humidity control”. X-ray diffraction, 3 ligands (GNP, MG, NA), 1 pocket (best druggability 0.52). MolNFT v1 #176517 on GenesisL1: 3D structure…

PDB: 7DPH
Type: protein
Length: 158 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase HRAS
EC: 3.6.5.2
UniProt: P01112
Ligands: GNP, MG, NA
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTPase HRAS (EC 3.6.5.2)	protein	158	32% helix, 26% strand	P01112

Ligands and binding sites

GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
NA · Sodium 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	169	0.52	0.79	30	MG, GNP

Compared structures

7DPH · H-Ras Q61H in complex with GppNHp (state 1) after structural transition by humidity… · 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 7DPH · PDBe 7DPH · UniProt P01112

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