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Crystal structure of human KRAS G12V mutant in complex with GDP

Analyse Crystal structure of human KRAS G12V mutant in complex with GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UQW
Type: protein
Length: 323 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase KRAS
EC: 3.6.5.-
UniProt: P01116
Ligands: GDP, MG
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTPase KRAS (EC 3.6.5.-)	protein	168	38% helix, 27% strand	P01116
B	GTPase KRAS (EC 3.6.5.-)	protein	155	34% helix, 27% 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

2 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	194	0.52	0.77	38	MG, GDP
2	219	0.51	0.76	40	MG, GDP

Interfaces

1 interface between chains.

A–B · 350 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

5UQW · Crystal structure of human KRAS G12V mutant in complex with GDP · 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 5UQW · PDBe 5UQW · UniProt P01116

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