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GFP-binding darpin fusion GC_R11

Analyse GFP-binding darpin fusion GC_R11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5MA3
Type
protein
Length
529 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Green fluorescent protein; R11
UniProt
P42212
Ligands
CRO
Pockets
5 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BGreen fluorescent proteinprotein22711% helix, 52% strandP42212
AR11protein30251% helix, 0% strand—

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 B
  • EDO · 1,2-ethanediol · additive · 6 copies · chains B, A

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1970.770.9726CRO
25480.710.8059empty
34860.680.7959EDO
42430.620.8139EDO
51210.490.8026empty

Interfaces

1 interface between chains.

  • B–A · 1595 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 cofactor (chromophore).

Compared structures

  • 5MA3 · GFP-binding DARPin fusion gc_R11 · the same entry in another collection · chain B against B, TM-score 1.00
  • P42212 · AlphaFold monomer V2.0 prediction for green fluorescent protein (P42212) · a predicted model of the same protein · chain B against A, TM-score 0.99

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