5INT

Crystal structure of the C-terminal Domain of Coenzyme A biosynthesis bifunctional protein CoaBC

PDB DOI: https://doi.org/10.2210/pdb5INT/pdb

Classification: LIGASE
Organism(s): Bacillus anthracis
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2016-03-07 Released: 2016-04-06
Deposition Author(s): Nocek, B., Zhou, M., Grimshaw, S., Kim, Y., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.15 Å
R-Value Free: 0.258
R-Value Work: 0.226
R-Value Observed: 0.227

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Crystal structure of the C-terminal Domain of Coenzyme A biosynthesis bifunctional protein CoaBC

Nocek, B., Zhou, M., Grimshaw, S., Anderson, W.F., Joachimiak, A.

To be published.

Macromolecule Content

Total Structure Weight: 49.62 kDa
Atom Count: 3,207
Modelled Residue Count: 394
Deposited Residue Count: 440
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Phosphopantothenate--cysteine ligase	A, B	220	Bacillus anthracis	Mutation(s): 0 Gene Names: coaBC, GBAA_4007, AB163_23415, AB164_18935, AB165_13850, AB166_05815, AB167_23710, AB168_27015, AB169_03120, AB170_11765... coaBC, GBAA_4007, AB163_23415, AB164_18935, AB165_13850, AB166_05815, AB167_23710, AB168_27015, AB169_03120, AB170_11765, AB171_07935, AB893_19460, ADK17_20550, ADT20_07585, ADT21_16720, BASH2_01930 EC: 6.3.2.5
UniProt
Find proteins for A0A6L8Q0G8 (Bacillus anthracis) Explore A0A6L8Q0G8 Go to UniProtKB: A0A6L8Q0G8
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	A0A6L8Q0G8
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: 2.15 Å
R-Value Free: 0.258
R-Value Work: 0.226
R-Value Observed: 0.227
Space Group: P 4 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 133.173	α = 90
b = 133.173	β = 90
c = 55.765	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
HKL-3000	data reduction
HKL-3000	data scaling
HKL-3000	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2016-04-06

Deposition Author(s):

Center for Structural Genomics of Infectious Diseases (CSGID)

Revision History (Full details and data files)

Version 1.0: 2016-04-06
Type: Initial release
Version 1.1: 2017-02-08
Changes: Structure summary
Version 1.2: 2017-11-01
Changes: Author supporting evidence
Version 1.3: 2018-09-19
Changes: Data collection, 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.