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NMR structure of the fifth domain of human BETA2-glycoprotein I

Analyse NMR structure of the fifth domain of human BETA2-glycoprotein I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1G4F
Type: protein
Length: 86 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BETA2-glycoprotein I
UniProt: P02749
Pockets: 1 · best druggability 0.47

Structure

solution nmr · 1 distinct chain · 8% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BETA2-glycoprotein I	protein	86	8% helix, 36% strand	P02749

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	158	0.47	0.76	28	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1G4F · NMR structure of the fifth domain of human BETA2-glycoprotein I · the same entry in another collection · chain A against A, TM-score 1.00
P02749 · AlphaFold monomer V2.0 prediction for beta-2-glycoprotein 1 (P02749) · a predicted model of the same protein · chain A against A, TM-score 0.83

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 P02749
Elsewhere: RCSB PDB 1G4F · PDBe 1G4F · UniProt P02749

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