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Crystal structure of an unusually linked dimeric variant of bet V 1 (B)

Analyse Crystal structure of an unusually linked dimeric variant of bet V 1 (B) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BKD
Type: protein
Length: 159 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major pollen allergen bet V 1-a
UniProt: P15494
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Major pollen allergen bet V 1-a	protein	159	26% helix, 40% strand	P15494

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	409	0.81	0.89	48	empty

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

4BKD · Crystal Structure of an unusually linked dimeric variant of Bet v 1 (b) · the same entry in another collection · chain A against A, TM-score 1.00
P15494 · AlphaFold monomer V2.0 prediction for major pollen allergen bet V 1-a (P15494) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P15494
Elsewhere: RCSB PDB 4BKD · PDBe 4BKD · UniProt P15494

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