GL1X · GenesisL1 explorer

Research workbench

Crystal structure of racemic dl-monellin in P-1

Analyse Crystal structure of racemic dl-monellin in P-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1KRL
Type
protein
Length
184 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Monellin, chain a; Monellin, chain B
UniProt
P02881, P02882

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CMonellin, chain aprotein440% helix, 61% strandP02881
B, DMonellin, chain Bprotein4835% helix, 35% strandP02882

Interfaces

2 interfaces between chains.

  • C–D · 1392 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 1386 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 1KRL · Crystal Structure of Racemic DL-monellin in P-1 · the same entry in another collection · chain A against A, TM-score 1.00
  • P02882 · AlphaFold monomer V2.0 prediction for monellin chain B (P02882) · a predicted model of the same protein · chain B against A, TM-score 0.91
  • P02881 · AlphaFold monomer V2.0 prediction for monellin chain a (P02881) · a predicted model of the same protein · chain A against A, TM-score 0.90

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.