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Pilotin from vibrio vulnificus type 2 secretion system, epss.

Analyse Pilotin from vibrio vulnificus type 2 secretion system, epss. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6I2V
Type: protein
Length: 110 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: A0A1V8MYF4
Ligands: SO4, SO3
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	110	45% helix, 31% strand	A0A1V8MYF4

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 copies · chains A
SO3 · Sulfite ion · ion · chains A
1PE · Pentaethylene glycol · additive · 5 copies · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

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	175	0.49	0.76	19	1PE

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6I2V · Pilotin from Vibrio vulnificus type 2 secretion system, EpsS. · 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 A0A1V8MYF4
Elsewhere: RCSB PDB 6I2V · PDBe 6I2V · UniProt A0A1V8MYF4

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