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Protein structure of USP from L. major in Apo-form

Analyse Protein structure of USP from L. major in Apo-form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OGZ
Type: protein
Length: 578 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.03
Source: Leishmania major
Molecule: UDP-sugar pyrophosphorylase
EC: 2.7.7.64
UniProt: D3G6S4
Pockets: 6 · best druggability 0.70

Structure

x-ray diffraction · resolution 2.03 · 1 distinct chain · 34% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	UDP-sugar pyrophosphorylase (EC 2.7.7.64)	protein	578	34% helix, 23% strand	D3G6S4

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	336	0.70	0.83	50	empty
2	517	0.64	0.76	43	empty
3	372	0.60	0.76	31	empty
4	237	0.49	0.74	26	empty
5	109	0.47	0.79	26	empty

Compared structures

3OGZ · Protein structure of usp from L. major in apo-form · 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 D3G6S4
Elsewhere: RCSB PDB 3OGZ · PDBe 3OGZ · UniProt D3G6S4

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