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Crystal structure of vpsu (VC0916) from vibrio cholerae

Analyse Crystal structure of vpsu (VC0916) from vibrio cholerae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6U1P
Type: protein
Length: 299 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Low molecular weight phosphotyrosine protein phosphatase
EC: 3.1.3.48
UniProt: A0A0H5WT43
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Low molecular weight phosphotyrosine protein phosphatase (EC 3.1.3.48)	protein	149	52% helix, 15% strand	A0A0H5WT43
B	Low molecular weight phosphotyrosine protein phosphatase (EC 3.1.3.48)	protein	150	51% helix, 15% strand	A0A0H5WT43

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains 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	79	0.32	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 2633 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6U1P · Crystal structure of VpsU (VC0916) from Vibrio cholerae · 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 A0A0H5WT43
Elsewhere: RCSB PDB 6U1P · PDBe 6U1P · UniProt A0A0H5WT43

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