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Crystal structure of oppa in a open conformation

Analyse Crystal structure of oppa in a open conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3FTO
Type
protein
Length
559 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Oligopeptide-binding protein oppa
UniProt
A2RJ53
Pockets
4 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOligopeptide-binding protein oppaprotein55929% helix, 23% strandA2RJ53

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19800.770.7965empty
22610.740.8840empty
3590.450.8418empty
4570.330.7719empty

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

  • 3FTO · Crystal structure of OppA in a open conformation · the same entry in another collection · chain A against A, TM-score 1.00

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