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Violacein biosynthetic enzyme vioe

Analyse Violacein biosynthetic enzyme vioe in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BMZ
Type: protein
Length: 375 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein
UniProt: Q7NSZ5
Pockets: 6 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein	protein	185	6% helix, 56% strand	Q7NSZ5
B	Putative uncharacterized protein	protein	190	6% helix, 54% strand	Q7NSZ5

Ligands and binding sites

PG4 · Tetraethylene glycol · additive · chains A
PGE · Triethylene glycol · additive · chains B

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

Pockets

6 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	402	0.70	0.82	66	empty
2	318	0.66	0.81	37	PG4
3	283	0.64	0.80	34	PGE
4	211	0.60	0.81	35	empty
5	81	0.37	0.77	17	empty

Interfaces

1 interface between chains.

A–B · 1775 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

3BMZ · Violacein biosynthetic enzyme VioE · 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 Q7NSZ5
Elsewhere: RCSB PDB 3BMZ · PDBe 3BMZ · UniProt Q7NSZ5

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