MolNFT v1 · #137483 · protein

Crystal structure of human KRAS G12A mutant in complex with GDP (edta soaked)

5VQ0 · GTPase KRAS: “Crystal structure of human KRAS G12A mutant in complex with GDP (edta soaked)”. X-ray diffraction, 2 ligands (GDP, MG), 3 pockets (best druggability 0.50). MolNFT v1 #137483 on GenesisL1: 3D structure, binding sites…

PDB: 5VQ0
Type: protein
Length: 320 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase KRAS
UniProt: P01116
Ligands: GDP, MG
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	GTPase KRAS	protein	160	36% helix, 26% strand	P01116

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	137	0.50	0.80	26	MG, GDP
2	131	0.48	0.79	24	MG, GDP
3	140	0.44	0.76	27	empty

Interfaces

1 interface between chains.

A–B · 1069 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

5VQ0 · Crystal structure of human KRAS G12A mutant in complex with GDP (EDTA soaked) · 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 P01116
Elsewhere: RCSB PDB 5VQ0 · PDBe 5VQ0 · UniProt P01116

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