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Crystal structure of the dark state of kindling fluorescent protein kfp from anemonia sulcata

Analyse Crystal structure of the dark state of kindling fluorescent protein kfp from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1XMZ
Type
protein
Length
455 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GFP-like chromoprotein FP595
Ligands
CRK, NH2
Pockets
5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGFP-like chromoprotein FP595protein2246% helix, 54% strand—
BGFP-like chromoprotein FP595protein2317% helix, 52% strand—

Ligands and binding sites

  • CRK · 4-{(Z)-[2-[3-(methylsulfanyl)propanoyl]-5-oxo-1-(2-oxoethyl)-1,5-dihydro-4H-imidazol-4-ylidene]methyl}benzenolate · ligand · 2 copies · chains A, B
  • NH2 · Amino group · ion · 2 copies · chains A, B
  • BME · Beta-mercaptoethanol · additive · 7 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1930.750.9726CRK
2750.740.9822CRK
3940.440.7915empty
4770.400.7917empty
5590.330.7610empty

Interfaces

1 interface between chains.

  • A–B · 992 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 covalent (additive adduct, covalent ligand).

Compared structures

  • 1XMZ · Crystal structure of the dark state of kindling fluorescent protein kfp from anemonia… · the same entry in another collection · chain B against B, TM-score 0.29

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