2CWN | pdb_00002cwn

Crystal structure of mouse transaldolase

PDB DOI: https://doi.org/10.2210/pdb2CWN/pdb

Classification: TRANSFERASE
Organism(s): Mus musculus
Mutation(s): Yes

Deposited: 2005-06-22 Released: 2005-12-22
Deposition Author(s): Handa, N., Arai, R., Nishino, A., Uchikubo, T., Takemoto, C., Morita, S., Kinoshita, Y., Nagano, Y., Uda, H., Terada, T., Shirouzu, M., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Free:
0.239 (Depositor)
R-Value Work:
0.196 (Depositor)
R-Value Observed:
0.196 (Depositor)

Starting Model: experimental
View more details

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

Crystal structure of mouse transaldolase

Handa, N., Arai, R., Nishino, A., Uchikubo, T., Takemoto, C., Morita, S., Kinoshita, Y., Nagano, Y., Uda, H., Terada, T., Shirouzu, M., Yokoyama, S.

To be published.

Macromolecule Content

Total Structure Weight: 72.99 kDa
Atom Count: 5,285
Modelled Residue Count: 633
Deposited Residue Count: 664
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Transaldolase	A, B	332	Mus musculus	Mutation(s): 1 EC: 2.2.1.2
UniProt
Find proteins for Q93092 (Mus musculus) Explore Q93092 Go to UniProtKB: Q93092
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q93092
Sequence Annotations Expand
Reference Sequence LOADING

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Free: 0.239 (Depositor)
R-Value Work: 0.196 (Depositor)
R-Value Observed: 0.196 (Depositor)

Space Group: P 2₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 79.05	α = 90
b = 108.009	β = 90
c = 75.608	γ = 90

Software Package:

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

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2005-12-22

Deposition Author(s):

RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Revision History (Full details and data files)

Version 1.0: 2005-12-22
Type: Initial release
Version 1.1: 2008-04-30
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2021-11-10
Changes: Database references
Version 1.4: 2023-10-25
Changes: Data collection, 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 R01GM157729.