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RSGREEN0.7-K206A-E222V in the green-on state

Analyse RSGREEN0.7-K206A-E222V in the green-on state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7A80
Type
protein
Length
905 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Green fluorescent protein
UniProt
A0A059PIQ0
Ligands
CRO, NO3
Pockets
11 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CGreen fluorescent proteinprotein22611% helix, 52% strandA0A059PIQ0
DGreen fluorescent proteinprotein22711% helix, 52% strandA0A059PIQ0

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 · 4 copies · chains A, B, C, D
  • NO3 · Nitrate ion · ion · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11340.800.9728CRO
21360.800.9730CRO
31300.790.9628CRO
41210.780.9726CRO
51880.480.7643empty

Interfaces

2 interfaces between chains.

  • C–D · 818 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 758 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 cofactor (chromophore).

Compared structures

  • 7A80 · rsGreen0.7-K206A-E222V in the green-on state · the same entry in another collection · chain A against A, TM-score 1.00

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