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Crystal structure of udp-glucose pyrophosphorylase V402W mutant from leishmania major

Analyse Crystal structure of udp-glucose pyrophosphorylase V402W mutant from leishmania… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NZH
Type: protein
Length: 965 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-glucose pyrophosphorylase
EC: 2.7.7.9
UniProt: Q4QDU3
Pockets: 12 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-glucose pyrophosphorylase (EC 2.7.7.9)	protein	483	33% helix, 26% strand	Q4QDU3
B	Udp-glucose pyrophosphorylase (EC 2.7.7.9)	protein	482	32% helix, 23% strand	Q4QDU3

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1047	0.74	0.77	111	empty
2	722	0.70	0.77	69	empty
3	429	0.65	0.78	47	empty
4	243	0.60	0.80	32	empty
5	51	0.58	0.91	16	empty

Interfaces

1 interface between chains.

A–B · 1616 Å² buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5NZH · Crystal structure of UDP-glucose pyrophosphorylase V402W mutant from Leishmania major · 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 Q4QDU3
Elsewhere: RCSB PDB 5NZH · PDBe 5NZH · UniProt Q4QDU3

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