› 4m2b

X-ray diffraction
2.2Å resolution

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

Released:
DOI: 10.2210/pdb4m2b/pdb
Model geometry
Fit model/data
PDB entry 4m2b coloured by chain, front view.
PDB entry 4m2b coloured by chain, side view.
PDB entry 4m2b coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Catalytic Mechanism and Allosteric Regulation of Udp-Glucose Pyrophosphorylase from Leishmania Major
Fuehring J, Routier FH, Lamerz A-C, Baruch P, Gerardy-Schahn R, Fedorov R
ACS Catalysis 36329 2976-2985 (2013)

Function and Biology Details

Reaction catalysed: 
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175696 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UTP--glucose-1-phosphate uridylyltransferase Chain: A
Molecule details ›
Chain: A
Length: 505 amino acids
Theoretical weight: 56.06 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4QDU3 (Residues: 1-494; Coverage: 100%)
Gene names: LMJF_18_0990, UGP
Sequence domains: UTP--glucose-1-phosphate uridylyltransferase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand UPG 1 x UPG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2221
Unit cell:
a: 78.79Å b: 86.9Å c: 138.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.175 0.242
Expression system: Escherichia coli

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