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1.7 ångström crystal structure of jun a 1, the major allergen from cedar pollen

Analyse 1.7 ångström crystal structure of jun a 1, the major allergen from cedar pollen in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PXZ
Type: protein
Length: 692 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major pollen allergen jun a 1
UniProt: P81294
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Major pollen allergen jun a 1	protein	346	11% helix, 37% strand	P81294

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	636	0.63	0.74	68	empty
2	69	0.37	0.78	17	empty
3	78	0.35	0.76	15	empty
4	82	0.33	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 223 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1PXZ · 1.7 Angstrom Crystal Structure of jun a 1, the major allergen from cedar pollen · the same entry in another collection · chain A against A, TM-score 1.00
P81294 · AlphaFold monomer V2.0 prediction for pectate lyase 1 (P81294) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P81294
Elsewhere: RCSB PDB 1PXZ · PDBe 1PXZ · UniProt P81294

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