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Periplasmic domain of epsl from vibrio parahaemolyticus

Analyse Periplasmic domain of epsl from vibrio parahaemolyticus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W7V
Type: protein
Length: 164 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: General secretion pathway protein L
UniProt: Q87TC9
Ligands: PO4
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	General secretion pathway protein L	protein	82	32% helix, 39% strand	Q87TC9

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.30	0.76	12	empty

Interfaces

1 interface between chains.

A–B · 469 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2W7V · periplasmic domain of EpsL from Vibrio parahaemolyticus · 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 Q87TC9
Elsewhere: RCSB PDB 2W7V · PDBe 2W7V · UniProt Q87TC9

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