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Crystal structure of kiwi-fruit allergen act D 2

Analyse Crystal structure of kiwi-fruit allergen act D 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BCT
Type: protein
Length: 201 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thaumatin-like protein
UniProt: P81370
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thaumatin-like protein	protein	201	14% helix, 38% strand	P81370

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

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	82	0.32	0.73	20	EPE

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

4BCT · Crystal structure of kiwi-fruit allergen Act d 2 · the same entry in another collection · chain A against A, TM-score 1.00
P81370 · AlphaFold monomer V2.0 prediction for thaumatin-like protein (P81370) · 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 P81370
Elsewhere: RCSB PDB 4BCT · PDBe 4BCT · UniProt P81370

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