3RMR | pdb_00003rmr

Crystal structure of Hyaloperonospora arabidopsidis ATR1 effector domain

PDB DOI: https://doi.org/10.2210/pdb3RMR/pdb

Classification: PROTEIN BINDING
Organism(s): Hyaloperonospora parasitica
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2011-04-21 Released: 2011-07-20
Deposition Author(s): Chou, S., Krasileva, K.V., Holton, J.M., Staskawicz, B.J., Alber, T.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free:
0.260 (Depositor), 0.260 (DCC)
R-Value Work:
0.223 (Depositor), 0.229 (DCC)
R-Value Observed:
0.225 (Depositor)

wwPDB Validation 3D Report Full Report

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

Literature

The Hyaloperonospora arabidopsidis ATR1 effector has distributed recognition surfaces and a structural subdomain conserved across oomycete species

Chou, S., Krasileva, K.V., Holton, J.M., Steinbrenner, A., Alber, T., Staskawicz, B.J.

To be published.

Macromolecule Content

Total Structure Weight: 89.03 kDa
Atom Count: 5,846
Modelled Residue Count: 702
Deposited Residue Count: 780
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Avirulence protein	A, B, C	260	Hyaloperonospora parasitica	Mutation(s): 0 Gene Names: Atr1, ATR1NdWsB
UniProt
Find proteins for M4B6G6 (Hyaloperonospora arabidopsidis (strain Emoy2)) Explore M4B6G6 Go to UniProtKB: M4B6G6
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	M4B6G6
Sequence Annotations Expand
Reference Sequence LOADING

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A, B, C	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.260 (Depositor), 0.260 (DCC)
R-Value Work: 0.223 (Depositor), 0.229 (DCC)
R-Value Observed: 0.225 (Depositor)

Space Group: P 6₁ 2 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 119.432	α = 90
b = 119.432	β = 90
c = 312.572	γ = 120

Software Package:

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

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2011-07-20

Deposition Author(s):

Krasileva, K.V.

Staskawicz, B.J.

Revision History (Full details and data files)

Version 1.0: 2011-07-20
Type: Initial release
Version 1.1: 2017-11-08
Changes: Refinement description
Version 1.2: 2019-07-17
Changes: Data collection, Derived calculations, Refinement description
Version 1.3: 2024-11-20
Changes: Data collection, Database references, Derived calculations, Structure summary

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 R01GM157729.