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Crystal structure of alternaria alternata major allergen alt a 1

Analyse Crystal structure of alternaria alternata major allergen alt a 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AUD
Type: protein
Length: 246 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major allergen alt a 1 subunit
UniProt: Q6Q128
Ligands: SO4
Pockets: 4 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Major allergen alt a 1 subunit	protein	123	0% helix, 52% strand	Q6Q128

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	80	0.47	0.81	17	empty
2	89	0.47	0.81	18	SO4
3	64	0.46	0.83	17	SO4
4	115	0.38	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 817 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 4 modified (disulfide, engineered).

Compared structures

4AUD · Crystal structure of alternaria alternata major allergen alt a 1 · 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
Every structure of UniProt Q6Q128
Elsewhere: RCSB PDB 4AUD · PDBe 4AUD · UniProt Q6Q128

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