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Crystal structure analysis of the dimeric form of the srcr domain of mouse marco

Analyse Crystal structure analysis of the dimeric form of the srcr domain of mouse marco in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2OYA
Type
protein
Length
204 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Macrophage receptor marco
UniProt
Q60754
Ligands
SO4
Pockets
1 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMacrophage receptor marcoprotein10219% helix, 35% strandQ60754

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11410.410.7413empty

Interfaces

1 interface between chains.

  • A–B · 1439 Ų buried · 30 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 2OYA · Crystal structure analysis of the dimeric form of the SRCR domain of mouse MARCO · the same entry in another collection · chain A against A, TM-score 1.00
  • Q60754 · AlphaFold monomer V2.0 prediction for macrophage receptor marco (Q60754) · a predicted model of the same protein · chain A against A, TM-score 0.87

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