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Open and closed structures of the udp-glucose pyrophosphorylase from leishmania major

Analyse Open and closed structures of the udp-glucose pyrophosphorylase from leishmania… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OEF
Type: protein
Length: 482 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: UTP-glucose-1-phosphate uridylyltransferase 2, putative
EC: 2.7.7.9
UniProt: Q4QDU3
Ligands: SO4
Pockets: 5 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	UTP-glucose-1-phosphate uridylyltransferase 2, putative (EC 2.7.7.9)	protein	482	31% helix, 26% strand	Q4QDU3

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

5 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	371	0.63	0.78	47	empty
2	466	0.59	0.75	56	SO4
3	255	0.54	0.76	35	empty
4	53	0.27	0.74	18	empty
5	56	0.27	0.73	15	empty

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

2OEF · Open and Closed Structures of the UDP-Glucose Pyrophosphorylase from Leishmania major · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q4QDU3
Elsewhere: RCSB PDB 2OEF · PDBe 2OEF · UniProt Q4QDU3

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