Research workbench

Structure of haze forming proteins in white wines: vitis vinifera thaumatin-like proteins

Analyse Structure of haze forming proteins in white wines: vitis vinifera… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4L5H
Type: protein
Length: 396 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: VVTL1
UniProt: O04708
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	VVTL1	protein	198	13% helix, 38% strand	O04708

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

3 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	196	0.47	0.75	24	empty
2	101	0.35	0.74	16	empty
3	92	0.32	0.73	19	empty

Interfaces

1 interface between chains.

A–B · 183 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

4L5H · Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins · 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 O04708
Elsewhere: RCSB PDB 4L5H · PDBe 4L5H · UniProt O04708

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.