3O0A | pdb_00003o0a

Crystal structure of the wild type CP1 hydrolitic domain from Aquifex Aeolicus leucyl-trna

PDB DOI: https://doi.org/10.2210/pdb3O0A/pdb

Classification: LIGASE
Organism(s): Aquifex aeolicus
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2010-07-19 Released: 2010-11-17
Deposition Author(s): Cura, V., Olieric, N., Wang, E.-D., Moras, D., Eriani, G., Cavarelli, J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.77 Å
R-Value Free:
0.225 (Depositor), 0.220 (DCC)
R-Value Work:
0.188 (Depositor), 0.190 (DCC)
R-Value Observed:
0.191 (Depositor)

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

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

Literature

Crystal Structure of the Wild Type and Two Mutants of the Cp1 Hydrolytic Domain from Aquifex Aeolicus Leucyl-tRNA Synthetase

Cura, V., Olieric, N., Guichard, A., Wang, E.-D., Moras, D., Eriani, G., Cavarelli, J.

To be published.

Macromolecule Content

Total Structure Weight: 49.79 kDa
Atom Count: 3,910
Modelled Residue Count: 425
Deposited Residue Count: 438
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Leucyl-tRNA synthetase subunit alpha	A, B	219	Aquifex aeolicus	Mutation(s): 0 Gene Names: leuS, aq_351 EC: 6.1.1.4
UniProt
Find proteins for O66680 (Aquifex aeolicus (strain VF5)) Explore O66680 Go to UniProtKB: O66680
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	O66680
Sequence Annotations Expand
Reference Sequence LOADING

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.77 Å
R-Value Free: 0.225 (Depositor), 0.220 (DCC)
R-Value Work: 0.188 (Depositor), 0.190 (DCC)
R-Value Observed: 0.191 (Depositor)

Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 38.689	α = 90
b = 98.18	β = 90
c = 116.667	γ = 90

Software Package:

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

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2010-11-17

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2010-11-17
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2023-09-06
Changes: Data collection, Database references, Refinement description
Version 1.3: 2024-10-30
Changes: 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.