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X-ray structure of the cyan fluorescent protein MTURQUOISE2 (K206A mutant)

Analyse X-ray structure of the cyan fluorescent protein MTURQUOISE2 (K206A mutant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ZTF
Type
protein
Length
236 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Green fluorescent protein
UniProt
P42212
Ligands
SWG
Pockets
1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGreen fluorescent proteinprotein23613% helix, 51% strandP42212

Ligands and binding sites

  • SWG · 2-[(4Z)-2-[(1R)-1-amino-2-hydroxy-ethyl]-4-(1H-indol-3-ylmethylidene)-5-oxo-imidazol-1-yl]ethanoic acid · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1730.720.9725SWG

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

  • 3ZTF · X-ray Structure of the Cyan Fluorescent Protein mTurquoise2 (K206A mutant) · the same entry in another collection · chain A against A, TM-score 1.00
  • P42212 · AlphaFold monomer V2.0 prediction for green fluorescent protein (P42212) · a predicted model of the same protein · chain A against A, TM-score 0.96

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