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Crystal structure of ara H 8.0201

Analyse Crystal structure of ara H 8.0201 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6V8M
Type: protein
Length: 303 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ara H 8 allergen isoform
UniProt: B0YIU5
Ligands: 2AN, SO4
Pockets: 2 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ara H 8 allergen isoform	protein	151	28% helix, 46% strand	B0YIU5
B	Ara H 8 allergen isoform	protein	152	27% helix, 47% strand	B0YIU5

Ligands and binding sites

2AN · 8-anilino-1-naphthalene sulfonate · ligand · 10 copies · chains A, B
SO4 · Sulfate ion · ion · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	561	0.84	0.89	57	2AN
2	577	0.84	0.89	60	2AN

Interfaces

1 interface between chains.

A–B · 753 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6V8M · Crystal structure of Ara h 8.0201 · 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 B0YIU5
Elsewhere: RCSB PDB 6V8M · PDBe 6V8M · UniProt B0YIU5

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