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Tannin acyl hydrolase from lactobacillus plantarum (native structure)

Analyse Tannin acyl hydrolase from lactobacillus plantarum (native structure) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J0C
Type: protein
Length: 910 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tannase
UniProt: B3Y018
Pockets: 13 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tannase	protein	452	36% helix, 18% strand	B3Y018
B	Tannase	protein	458	35% helix, 20% strand	B3Y018

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains A, B
1PE · Pentaethylene glycol · additive · chains B

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

Pockets

13 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	309	0.61	0.79	42	PEG
2	272	0.58	0.78	43	empty
3	82	0.50	0.83	18	PEG
4	233	0.49	0.75	44	empty
5	94	0.36	0.75	25	empty

Interfaces

1 interface between chains.

A–B · 784 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4J0C · tannin acyl hydrolase from Lactobacillus plantarum (native structure) · 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 B3Y018
Elsewhere: RCSB PDB 4J0C · PDBe 4J0C · UniProt B3Y018

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