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Crystal structure of the human NRAS GTPase bound with GDP

Analyse Crystal structure of the human NRAS GTPase bound with GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CON
Type: protein
Length: 156 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase NRAS
UniProt: P01111
Ligands: GDP, MG, UNX
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTPase NRAS	protein	156	35% helix, 27% strand	P01111

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · 4 copies · chains A
UNX · Unknown atom or ion · ion · 8 copies · 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	132	0.45	0.77	27	MG, GDP

Compared structures

3CON · Crystal structure of the human NRAS GTPase bound with GDP · the same entry in another collection · chain A against A, TM-score 1.00
P01111 · AlphaFold monomer V2.0 prediction for GTPase NRAS (P01111) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P01111
Elsewhere: RCSB PDB 3CON · PDBe 3CON · UniProt P01111

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