1XSV

X-ray crystal structure of conserved hypothetical UPF0122 protein SAV1236 from Staphylococcus aureus subsp. aureus Mu50

PDB DOI: https://doi.org/10.2210/pdb1XSV/pdb

Classification: UNKNOWN FUNCTION
Organism(s): Staphylococcus aureus
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2004-10-20 Released: 2004-10-26
Deposition Author(s): Walker, J.R., Xu, X., Virag, C., McDonald, M.-L., Houston, S., Buzadzija, K., Vedadi, M., Dharamsi, A., Fiebig, K.M., Savchenko, A.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.70 Å
R-Value Free: 0.224
R-Value Work: 0.187
R-Value Observed: 0.187

wwPDB Validation 3D Report Full Report

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

Literature

1.7 Angstrom Crystal Structure of Conserved Hypothetical UPF0122 Protein SAV1236 From Staphylococcus aureus

Walker, J.R., Xu, X., Virag, C., McDonald, M.-L., Houston, S., Buzadzija, K., Vedadi, M., Dharamsi, A., Fiebig, K.M., Savchenko, A.

To be published.

Macromolecule Content

Total Structure Weight: 27.94 kDa
Atom Count: 2,130
Modelled Residue Count: 212
Deposited Residue Count: 226
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Hypothetical UPF0122 protein SAV1236	A, B	113	Staphylococcus aureus	Mutation(s): 2 Gene Names: SAV1236
UniProt
Find proteins for P67248 (Staphylococcus aureus (strain Mu50 / ATCC 700699)) Explore P67248 Go to UniProtKB: P67248
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P67248
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: 1.70 Å
R-Value Free: 0.224
R-Value Work: 0.187
R-Value Observed: 0.187
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 37.096	α = 90
b = 67.784	β = 90
c = 87.978	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
HKL-2000	data reduction
SCALEPACK	data scaling
SOLVE	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2004-10-26

Deposition Author(s):

McDonald, M.-L.

Revision History (Full details and data files)

Version 1.0: 2004-10-26
Type: Initial release
Version 1.1: 2008-04-30
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.