5EUR

Hypothetical protein SF216 from shigella flexneri 5a M90T

PDB DOI: https://doi.org/10.2210/pdb5EUR/pdb

Classification: UNKNOWN FUNCTION
Organism(s): Shigella flexneri 5a str. M90T
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2015-11-19 Released: 2016-11-23
Deposition Author(s): Lee, Y.-S., Seok, S.-H., Kim, H.-N., An, J.-G., Chung, K.Y., Won, H.-S., Seo, M.-D.
Funding Organization(s): National Research Foundation of Korea

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.70 Å
R-Value Free: 0.240
R-Value Work: 0.205
R-Value Observed: 0.206

wwPDB Validation 3D Report Full Report

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

Literature

Crystal structure of SF216 from Shigella flexneri strain 5a

Lee, Y.-S., Seok, S.-H., Kim, H.-N., An, J.-G., Chung, K.Y., Won, H.-S., Seo, M.-D.

To be published.

Macromolecule Content

Total Structure Weight: 45.85 kDa
Atom Count: 2,947
Modelled Residue Count: 334
Deposited Residue Count: 408
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Uncharacterized protein	A, B, C	136	Shigella flexneri 5a str. M90T	Mutation(s): 0 Gene Names: SF5M90T_216
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
SO4 Query on SO4 Download Ideal Coordinates CCD File SDF format, chain E [auth A] MOL2 format, chain E [auth A]	E [auth A]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain E [auth A] Interactions & Density Focus chain E [auth A]
MG Query on MG Download Ideal Coordinates CCD File SDF format, chain D [auth A] MOL2 format, chain D [auth A]	D [auth A]	MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N		Interactions Focus chain D [auth A] Interactions & Density Focus chain D [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.70 Å
R-Value Free: 0.240
R-Value Work: 0.205
R-Value Observed: 0.206
Space Group: C 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 87.399	α = 90
b = 50.411	β = 104.1
c = 99.921	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
PHENIX	model building
PHENIX	phasing
HKL-2000	data scaling

Structure Validation

View Full Validation Report

Entry History & Funding Information

Deposition Data

Released Date: 2016-11-23

Deposition Author(s):

Funding Organization	Location	Grant Number
National Research Foundation of Korea	Korea, Republic Of	2012R1A1A1039738
National Research Foundation of Korea	Korea, Republic Of	2014R1A1A2054691

Revision History (Full details and data files)

Version 1.0: 2016-11-23
Type: Initial release
Version 1.1: 2017-10-04
Changes: Data collection, Derived calculations
Version 1.2: 2024-03-20
Changes: Data collection, Database references

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.