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Structure of M-csf bound to the first three domains of fms

Analyse Structure of M-csf bound to the first three domains of fms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3EJJ
Type
protein
Length
565 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Colony stimulating factor-1; Macrophage colony-stimulating factor 1 receptor
EC
2.7.10.1
UniProt
Q3U395, P09581
Ligands
NAG
Pockets
4 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 30% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AColony stimulating factor-1protein14854% helix, 8% strandQ3U395
BColony stimulating factor-1protein14552% helix, 8% strandQ3U395
XMacrophage colony-stimulating factor 1 receptor (EC 2.7.10.1)protein2725% helix, 51% strandP09581

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains X

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16230.750.8170empty
21770.510.7821empty
3660.490.8517empty
4530.260.7414empty

Interfaces

2 interfaces between chains.

  • A–X · 987 Ų buried · 11 hydrogen bonds · protein-protein
  • A–B · 807 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 3EJJ · Structure of M-CSF bound to the first three domains of FMS · the same entry in another collection · chain A against A, TM-score 1.00
  • P09581 · AlphaFold monomer V2.0 prediction for macrophage colony-stimulating factor 1 receptor… · a predicted model of the same protein · chain X against A, TM-score 0.64

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