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Crystal structure of a monomeric FLT3 ligand variant

Analyse Crystal structure of a monomeric FLT3 ligand variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NBI
Type
protein
Length
269 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fms-related tyrosine kinase 3 ligand
UniProt
P49771
Ligands
SO4
Pockets
2 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFms-related tyrosine kinase 3 ligandprotein13153% helix, 8% strandP49771
BFms-related tyrosine kinase 3 ligandprotein13851% helix, 10% strandP49771

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 5 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11510.460.7634empty
21140.430.7728empty

Interfaces

1 interface between chains.

  • A–B · 640 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 7NBI · Crystal structure of a monomeric FLT3 Ligand variant · the same entry in another collection · chain A against A, TM-score 1.00
  • P49771 · AlphaFold monomer V2.0 prediction for fms-related tyrosine kinase 3 ligand (P49771) · a predicted model of the same protein · chain A against A, TM-score 0.93

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