Research workbench

KRAS G12V and H-REV107 peptide complex

Analyse KRAS G12V and H-REV107 peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7C41
Type: protein
Length: 682 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P01116, P53816
Ligands: GDP, MG

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, J, M, G	—	protein	168	—	P01116
D	—	protein	10	—	P53816

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 4 copies · chains A, D, J, M, G
MG · Magnesium ion · metal · 4 copies · chains A, D, J, M, G

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

Compared structures

7C41 · KRAS G12V and H-REV107 peptide complex · the same entry in another collection · chain A against A, TM-score 1.00
P53816 · AlphaFold monomer V2.0 prediction for phospholipase a and acyltransferase 3 (P53816) · a predicted model of the same protein · chain D against A, TM-score 0.41

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
Every structure of UniProt P53816
Elsewhere: RCSB PDB 7C41 · PDBe 7C41 · UniProt P01116 · UniProt P53816

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