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Tannin acyl hydrolase in complex with gallic acid

Analyse Tannin acyl hydrolase in complex with gallic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J0H
Type: protein
Length: 940 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tannase
UniProt: B3Y018
Ligands: GDE
Pockets: 12 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tannase	protein	470	34% helix, 21% strand	B3Y018

Ligands and binding sites

GDE · 3,4,5-trihydroxybenzoic acid · ligand · 2 copies · chains A, B
PEG · Di(hydroxyethyl)ether · additive · 7 copies · chains A, B
PG4 · Tetraethylene glycol · additive · 2 copies · chains A, B

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

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	435	0.61	0.76	40	GDE
2	403	0.58	0.75	42	GDE
3	333	0.57	0.76	41	empty
4	284	0.53	0.75	34	empty
5	130	0.39	0.74	24	empty

Interfaces

1 interface between chains.

A–B · 713 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4J0H · Tannin acyl hydrolase in complex with gallic acid · 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 4J0H · PDBe 4J0H · UniProt B3Y018

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