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Crystal structure of Uso1-2

Analyse Crystal structure of Uso1-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LSU
Type: protein
Length: 676 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.7
Source: Saccharomyces cerevisiae S288c
Molecule: Intracellular protein transport protein USO1
UniProt: P25386
Pockets: 5 · best druggability 0.62

Structure

x-ray diffraction · resolution 2.7 · 1 distinct chain · 65% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Intracellular protein transport protein USO1	protein	676	65% helix, 2% strand	P25386

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	317	0.62	0.79	50	empty
2	76	0.33	0.75	19	empty
3	58	0.32	0.76	13	empty
4	69	0.31	0.75	16	empty
5	50	0.29	0.76	12	empty

Compared structures

6LSU · Crystal structure of USO1-2 · the same entry in another collection · chain A against A, TM-score 1.00
P25386 · AlphaFold monomer V2.0 prediction for intracellular protein transport protein USO1… · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P25386
Elsewhere: RCSB PDB 6LSU · PDBe 6LSU · UniProt P25386

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