2OSU

Probable glutaminase from Bacillus subtilis complexed with 6-diazo-5-oxo-L-norleucine

PDB DOI: https://doi.org/10.2210/pdb2OSU/pdb

Classification: HYDROLASE
Organism(s): Bacillus subtilis
Expression System: Escherichia coli BL21(DE3)
Mutation(s): Yes

Deposited: 2007-02-06 Released: 2007-03-06
Deposition Author(s): Kim, Y., Dementieva, I., Vinokour, E., Collart, F., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.29 Å
R-Value Free: 0.252
R-Value Work: 0.194
R-Value Observed: 0.200

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

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

Literature

The structure of probable glutaminase from B. subtilis complexed with its inhibitor 6-diazo-5-oxo-L-norleucine

Kim, Y., Dementieva, I., Vinokour, E., Collart, F., Joachimiak, A.

To be published.

Macromolecule Content

Total Structure Weight: 74.47 kDa
Atom Count: 5,030
Modelled Residue Count: 609
Deposited Residue Count: 660
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Glutaminase 1	A, B	330	Bacillus subtilis	Mutation(s): 12 Gene Names: glsA1, glsA, BSU02430 EC: 3.5.1.2
UniProt
Find proteins for O31465 (Bacillus subtilis (strain 168)) Explore O31465 Go to UniProtKB: O31465
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	O31465
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
DON Query on DON Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth B]	C [auth A], D [auth B]	6-DIAZENYL-5-OXO-L-NORLEUCINE C₆ H₁₁ N₃ O₃ CKRLZVNSTCQAJW-YFKPBYRVSA-N		Interactions Focus chain C [auth A] Focus chain D [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth B]

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: 2.29 Å
R-Value Free: 0.252
R-Value Work: 0.194
R-Value Observed: 0.200
Space Group: P 2₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 71.247	α = 90
b = 184.701	β = 90
c = 51.422	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
SBC-Collect	data collection
HKL-2000	data collection
HKL-2000	data reduction
HKL-2000	data scaling
HKL-3000	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2007-03-06

Deposition Author(s):

Midwest Center for Structural Genomics (MCSG)

Revision History (Full details and data files)

Version 1.0: 2007-03-06
Type: Initial release
Version 1.1: 2007-11-20
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

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.