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Structure of a sych-yoph chaperone-effector complex

Analyse Structure of a sych-yoph chaperone-effector complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4GF3
Type
protein
Length
151 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative yoph targeting protein; Tyrosine-protein phosphatase yoph
UniProt
Q7BTX0, P15273
Pockets
2 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative yoph targeting proteinprotein12331% helix, 29% strandQ7BTX0
BTyrosine-protein phosphatase yophprotein2846% helix, 29% strandP15273

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.380.8017empty
2600.350.7612empty

Interfaces

1 interface between chains.

  • A–B · 993 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 4GF3 · Structure of a SycH-YopH Chaperone-Effector Complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P15273 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase yoph (P15273) · a predicted model of the same protein · chain B against A, TM-score 0.55

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