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Thaumatin structure determined at room temperature by in-situ diffraction in chipx

Analyse Thaumatin structure determined at room temperature by in-situ diffraction in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZEJ
Type: protein
Length: 207 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thaumatin-1
UniProt: P02883
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thaumatin-1	protein	207	12% helix, 39% strand	P02883

Ligands and binding sites

TLA · L(+)-tartaric 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.55	0.90	19	empty

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

3ZEJ · Thaumatin structure determined at room temperature by in-situ diffraction in ChipX · 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 P02883
Elsewhere: RCSB PDB 3ZEJ · PDBe 3ZEJ · UniProt P02883

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