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3D NMR structure of the cytoplasmic rhodanese domain of the full- length inner membrane protein ygap from escherichia COLI

Analyse 3D NMR structure of the cytoplasmic rhodanese domain of the full- length inner… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2MOL
Type
protein
Length
108 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Inner membrane protein ygap
UniProt
P55734
Pockets
2 · best druggability 0.59

Structure

solution nmr · 1 distinct chain · 29% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInner membrane protein ygapprotein10829% helix, 16% strandP55734

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1870.590.8725empty
2840.340.7417empty

Compared structures

  • 2MOL · 3D NMR structure of the cytoplasmic rhodanese domain of the full-length inner membrane… · the same entry in another collection · chain A against A, TM-score 1.00
  • P55734 · AlphaFold monomer V2.0 prediction for inner membrane protein ygap (P55734) · a predicted model of the same protein · chain A against A, TM-score 0.81

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