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Crystal structure of GFP S205A/T203V at 2.2 a resolution

Analyse Crystal structure of GFP S205A/T203V at 2.2 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4OGS
Type
protein
Length
450 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Green fluorescent protein
UniProt
P42212
Ligands
CRO, CL
Pockets
7 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGreen fluorescent proteinprotein2259% helix, 53% strandP42212
BGreen fluorescent proteinprotein2259% 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 · 2 copies · chains A, B
  • CL · Chloride ion · ion · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11050.780.9828CRO
2820.760.9825CRO
32310.510.7634empty
41900.490.7628empty
5880.340.7417empty

Interfaces

1 interface between chains.

  • A–B · 894 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor (chromophore).

Compared structures

  • 4OGS · Crystal structure of GFP S205A/T203V at 2.2 A resolution · 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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