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Atomic resolution structure of GFP measured on a rotating anode

Analyse Atomic resolution structure of GFP measured on a rotating anode in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2WUR
Type
protein
Length
226 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Green fluorescent protein
UniProt
P42212
Ligands
GYS
Pockets
1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGreen fluorescent proteinprotein22612% helix, 51% strandP42212

Ligands and binding sites

  • GYS · [(4Z)-2-(1-amino-2-hydroxyethyl)-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid · ligand · chains A
  • EOH · Ethanol · additive · 7 copies · chains A
  • IPA · Isopropyl alcohol · additive · 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
1940.770.9827GYS

Modifications

Observed in the structure: 2 cofactor (chromophore).

Compared structures

  • 2WUR · Atomic resolution structure of GFP measured on a rotating anode · 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 0.99

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