3LG3

1.4A Crystal Structure of Isocitrate Lyase from Yersinia pestis CO92

PDB DOI: https://doi.org/10.2210/pdb3LG3/pdb

Classification: LYASE
Organism(s): Yersinia pestis
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2010-01-19 Released: 2010-04-14
Deposition Author(s): Sharma, S.S., Brunzelle, J.S., Skarina, T., Savchenko, A., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.40 Å
R-Value Free: 0.165
R-Value Work: 0.131
R-Value Observed: 0.133

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

1.4A Crystal Structure of Isocitrate Lyase from Yersinia pestis CO92

Sharma, S.S., Brunzelle, J.S., Wawrzak, Z., Skarina, T., Gordon, E., Savchenko, A., Anderson, W.F.

To be published.

Macromolecule Content

Total Structure Weight: 96.37 kDa
Atom Count: 7,874
Modelled Residue Count: 833
Deposited Residue Count: 870
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Isocitrate lyase	A, B	435	Yersinia pestis	Mutation(s): 0 Gene Names: aceA, y0016, YPO3725, YP_3087 EC: 4.1.3.1
UniProt
Find proteins for A0A2S9PCG6 (Yersinia pestis) Explore A0A2S9PCG6 Go to UniProtKB: A0A2S9PCG6
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	A0A2S9PCG6
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A, B	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.40 Å
R-Value Free: 0.165
R-Value Work: 0.131
R-Value Observed: 0.133
Space Group: C 2 2 2₁
Diffraction Data: https://doi.org/10.18430/M33LG3

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 94.163	α = 90
b = 115.133	β = 90
c = 174.835	γ = 90

Software Package:

Software Name	Purpose
BLU-MAX	data collection
CRANK	phasing
ARP/wARP	model building
PHENIX	refinement
HKL-2000	data reduction
HKL-2000	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2010-04-14

Deposition Author(s):

Brunzelle, J.S.

Center for Structural Genomics of Infectious Diseases (CSGID)

Revision History (Full details and data files)

Version 1.0: 2010-04-14
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2011-12-14
Changes: Structure summary

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.