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Crystal structure of red fluorescent gene-engineered variant with improved folding - LANRFP_DELS83 (branchiostoma lanceolatum)

Analyse Crystal structure of red fluorescent gene-engineered variant with improved… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4JGE
Type
protein
Length
431 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Red fluorescent protein blfp-R5
UniProt
B1PND0
Ligands
CR2
Pockets
3 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARed fluorescent protein blfp-R5protein2159% helix, 56% strandB1PND0
BRed fluorescent protein blfp-R5protein2169% helix, 55% strandB1PND0

Ligands and binding sites

  • CR2 · {(4Z)-2-(aminomethyl)-4-[(4-hydroxyphenyl)methylidene]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · 2 copies · chains A, B
  • GOL · Glycerol · additive · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11850.610.8328empty
2800.360.7617GOL
3800.350.7616empty

Interfaces

1 interface between chains.

  • A–B · 1029 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 cofactor (chromophore).

Compared structures

  • 4JGE · Crystal structure of red fluorescent gene-engineered variant with improved folding… · the same entry in another collection · chain A against A, TM-score 1.00

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