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Crystal Structure of the four Ig-like domain of LILRB2(LIR2/ILT4/CD85d)

Analyse Crystal Structure of the four Ig-like domain of LILRB2(LIR2/ILT4/CD85d) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AED
Type: protein
Length: 389 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.797
Source: Homo sapiens
Molecule: Leukocyte immunoglobulin-like receptor subfamily B member 2
UniProt: Q8N423
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · resolution 3.797 · 1 distinct chain · 2% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Leukocyte immunoglobulin-like receptor subfamily B member 2	protein	389	2% helix, 49% strand	Q8N423

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.41	0.81	11	empty
2	89	0.37	0.76	20	empty
3	74	0.36	0.76	14	empty

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

6AED · Crystal structure of the four ig-like domain of LILRB2(LIR2/ILT4/CD85D) · the same entry in another collection · chain A against A, TM-score 1.00
Q8N423 · AlphaFold monomer V2.0 prediction for leukocyte immunoglobulin-like receptor subfamily B… · a predicted model of the same protein · chain A against A, TM-score 0.92

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8N423
Elsewhere: RCSB PDB 6AED · PDBe 6AED · UniProt Q8N423

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