MolNFT v1 · #138636 · protein

KRAS G12V, bound to gppnhp and miniprotein 225-11(A30R)

5WPM · GTPase KRAS: “KRAS G12V, bound to gppnhp and miniprotein 225-11(A30R)”. X-ray diffraction, 3 ligands (GNP, MG, SO4). MolNFT v1 #138636 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5WPM
Type: protein
Length: 214 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase KRAS; RAS binding peptide
UniProt: P01116
Ligands: GNP, MG, SO4

Structure

x-ray diffraction · 3 distinct chains · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTPase KRAS	protein	153	38% helix, 25% strand	P01116
B	RAS binding peptide	protein	30	60% helix, 0% strand	—
C	RAS binding peptide	protein	31	58% helix, 0% strand	—

Ligands and binding sites

GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · chains C

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

Interfaces

3 interfaces between chains.

A–B · 879 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 842 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 258 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5WPM · KRas G12V, bound to GppNHp and miniprotein 225-11(A30R) · 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 5WPM · PDBe 5WPM · UniProt P01116

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