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Crystal structure of L281D mutant of udp-glucose pyrophosphorylase from leishmania major in complex with udp-glc

Analyse Crystal structure of L281D mutant of udp-glucose pyrophosphorylase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4M2B
Type: protein
Length: 483 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-glucose pyrophosphorylase
EC: 2.7.7.9
UniProt: Q4QDU3
Ligands: UPG
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-glucose pyrophosphorylase (EC 2.7.7.9)	protein	483	34% helix, 24% strand	Q4QDU3

Ligands and binding sites

UPG · Uridine-5'-diphosphate-glucose · ligand · chains A

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

Pockets

4 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	898	0.78	0.81	80	UPG
2	80	0.34	0.75	23	empty
3	82	0.33	0.74	18	empty
4	63	0.31	0.75	17	empty

Compared structures

4M2B · Crystal structure of L281D mutant of udp-glucose pyrophosphorylase 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 4M2B · PDBe 4M2B · UniProt Q4QDU3

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