4J18

Crystal structure of H191L mutant of UDP-glucose pyrophosphorylase from Leishmania major

PDB DOI: https://doi.org/10.2210/pdb4J18/pdb

Classification: TRANSFERASE
Organism(s): Leishmania major
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2013-02-01 Released: 2014-01-29
Deposition Author(s): Fuehring, J.I., Routier, F.H., Lamerz, A.-C., Baruch, P., Gerardy-Schahn, R., Fedorov, R.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.35 Å
R-Value Free: 0.232
R-Value Work: 0.178
R-Value Observed: 0.181

wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

Catalytic Mechanism and Allosteric Regulation of UDP-Glucose Pyrophosphorylase from Leishmania major

Fuehring, J.I., Routier, F.H., Lamerz, A.-C., Baruch, P., Gerardy-Schahn, R., Fedorov, R.

(2013) ACS Catal 3: 2976-2985

DOI: https://doi.org/10.1021/cs4007777

Macromolecule Content

Total Structure Weight: 56.03 kDa
Atom Count: 4,053
Modelled Residue Count: 485
Deposited Residue Count: 505
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
UDP-glucose pyrophosphorylase	A	505	Leishmania major	Mutation(s): 1 Gene Names: UGP, LMJF_18_0990 EC: 2.7.7.9
UniProt
Find proteins for Q4QDU3 (Leishmania major) Explore Q4QDU3 Go to UniProtKB: Q4QDU3
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q4QDU3
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.35 Å
R-Value Free: 0.232
R-Value Work: 0.178
R-Value Observed: 0.181
Space Group: P 4₃

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 101.31	α = 90
b = 101.31	β = 90
c = 71.77	γ = 90

Software Package:

Software Name	Purpose
MxCuBE	data collection
AMoRE	phasing
REFMAC	refinement
XDS	data reduction
XSCALE	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2014-01-29

Deposition Author(s):

Gerardy-Schahn, R.

Revision History (Full details and data files)

Version 1.0: 2014-01-29
Type: Initial release
Version 1.1: 2023-09-20
Changes: Data collection, Database references, Refinement description

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.