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Crystal structure of human beta-2-glycoprotein-I (apolipoprotein-H)

Analyse Crystal structure of human beta-2-glycoprotein-I (apolipoprotein-H) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1C1Z
Type: protein
Length: 326 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BETA2-glycoprotein-I
Ligands: NAG, NDG, BMA, MAN
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BETA2-glycoprotein-I	protein	326	2% helix, 40% strand	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 2 copies · chains A
BMA · beta-D-mannopyranose · sugar · 2 copies
MAN · alpha-D-mannopyranose · sugar · 2 copies

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.40	0.81	19	empty

Modifications

Observed in the structure: 4 glycan, 3 disulfide (N-glycosylation, disulfide).

Compared structures

1C1Z · Crystal structure of human beta-2-glycoprotein-I (apolipoprotein-H) · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 1C1Z · PDBe 1C1Z

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