6K2F

Structure of Eh TWINFILIN

PDB DOI: https://doi.org/10.2210/pdb6K2F/pdb

Classification: STRUCTURAL PROTEIN
Organism(s): Entamoeba histolytica HM-1:IMSS
Expression System: Escherichia coli BL21
Mutation(s): No

Deposited: 2019-05-14 Released: 2020-06-03
Deposition Author(s): Kumar, N., Gourinath, S., Rath, P.P.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.55 Å
R-Value Free: 0.187
R-Value Work: 0.166
R-Value Observed: 0.167

wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

Structure of N-terminal Twinfilin domain from Entamoeba histolytica

Kumar, N., Gourinath, S.

To be published.

Macromolecule Content

Total Structure Weight: 31.52 kDa
Atom Count: 2,369
Modelled Residue Count: 276
Deposited Residue Count: 276
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Actin binding protein family protein	A, B	138	Entamoeba histolytica HM-1:IMSS	Mutation(s): 0
UniProt
Find proteins for N9V330 (Entamoeba histolytica HM-1:IMSS-A) Explore N9V330 Go to UniProtKB: N9V330
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	N9V330
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.55 Å
R-Value Free: 0.187
R-Value Work: 0.166
R-Value Observed: 0.167
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 34.71	α = 90
b = 86.544	β = 90
c = 88.06	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
HKL-2000	data reduction
SCALEPACK	data scaling
PHASER	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2020-06-03

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2020-06-03
Type: Initial release
Version 1.1: 2023-11-22
Changes: Data collection, Database references, Refinement description

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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.