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NMR2 Structure of KRAS G12V (GMPPNP bound) in complex with 5-(1H-indol-2-l)piperazin-2-one

Analyse NMR2 Structure of KRAS G12V (GMPPNP bound) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8PI0
Type: protein
Length: 168 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: NOT
Source: Homo sapiens
Molecule: V-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog, isoform CRA_b
UniProt: A0A024RAV5
Ligands: YVW
Pockets: 5 · best druggability 0.78

Structure

solution nmr · resolution NOT · 1 distinct chain · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	V-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog, isoform CRA_b	protein	168	37% helix, 23% strand	A0A024RAV5

Ligands and binding sites

YVW · (5~{S})-5-(1~{H}-indol-2-yl)piperazin-2-one · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	103	0.78	0.97	35	empty
2	137	0.66	0.88	28	YVW
3	111	0.61	0.86	32	empty
4	50	0.33	0.78	12	empty
5	53	0.33	0.78	16	empty

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 A0A024RAV5
Elsewhere: RCSB PDB 8PI0 · PDBe 8PI0 · UniProt A0A024RAV5

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