Research workbench

Crystal structure of human KRAS G12A mutant in complex with GTP

Analyse Crystal structure of human KRAS G12A mutant in complex with GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VPI
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase KRAS
UniProt: P01116
Ligands: GTP, MG
Pockets: 4 · best druggability 0.53

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	GTPase KRAS	protein	159	36% helix, 26% strand	P01116

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · 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

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	185	0.53	0.79	29	GTP, MG
2	167	0.51	0.79	29	GTP, MG
3	81	0.44	0.80	29	empty
4	72	0.30	0.74	22	empty

Interfaces

1 interface between chains.

A–B · 1006 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

5VPI · Crystal structure of human KRAS G12A mutant in complex with GTP · 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 5VPI · PDBe 5VPI · UniProt P01116

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.