MolNFT v1 · #128845 · protein

Human KRAS in complex with darpin K27

5O2T · GTPase KRAS: “Human KRAS in complex with darpin K27”. X-ray diffraction, 3 ligands (GSP, MG, SO4), 3 pockets (best druggability 0.68). MolNFT v1 #128845 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5O2T
Type: protein
Length: 306 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase KRAS; Darpin 55
UniProt: P01116
Ligands: GSP, MG, SO4
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTPase KRAS	protein	164	38% helix, 27% strand	P01116
B	Darpin 55	protein	142	51% helix, 0% strand	—

Ligands and binding sites

GSP · 5'-guanosine-diphosphate-monothiophosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
SO4 · Sulfate ion · ion · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	412	0.68	0.80	44	MG, GSP
2	79	0.63	0.91	20	empty
3	56	0.45	0.84	15	empty

Interfaces

1 interface between chains.

A–B · 953 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

5O2T · Human KRAS in complex with darpin K27 · 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 5O2T · PDBe 5O2T · UniProt P01116

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