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Green fluorescent protein (GFP) from aequorea victoria, gln 80 replaced with arg

Analyse Green fluorescent protein (GFP) from aequorea victoria, gln 80 replaced with arg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGreen fluorescent proteinprotein22511% helix, 52% strandP42212

Ligands and binding sites

  • CRO · {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11020.770.9826CRO
2620.350.7811empty

Modifications

Observed in the structure: 2 cofactor (chromophore).

Compared structures

  • 1EMB · Green fluorescent protein (GFP) from aequorea victoria, gln 80 replaced with arg · 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 1.00

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