3N4G

Crystal structure of native Cg10062

PDB DOI: https://doi.org/10.2210/pdb3N4G/pdb

Classification: HYDROLASE
Organism(s): Corynebacterium glutamicum
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2010-05-21 Released: 2011-06-01
Deposition Author(s): Guo, Y., Robertson, B.A., Hackert, M.L., Whitman, C.P.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.44 Å
R-Value Free: 0.259
R-Value Work: 0.209
R-Value Observed: 0.211

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

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

Literature

Crystal Structures of the Native and Inactivated Cg10062, a cis-3-Chloroacrylic Acid Dehalogenase from Corynebacterium glutamicum: Implications for the Evolution of cis-3-Chloroacrylic Acid Dehalogenase Activity in the Tautomerase Superfamily

Guo, Y., Robertson, B.A., J Poelarends, G., Thunnissen, A.-M.W.H., Whitman, C.P., Hackert, M.L., Dijkstra, B.W.

To be published.

Macromolecule Content

Total Structure Weight: 51.35 kDa
Atom Count: 3,692
Modelled Residue Count: 432
Deposited Residue Count: 444
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Putative tautomerase	A, B, C	148	Corynebacterium glutamicum	Mutation(s): 0 Gene Names: cg0081, Cg10062, Cgl0062 EC: 3.8.1
UniProt
Find proteins for Q8NU77 (Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)) Explore Q8NU77 Go to UniProtKB: Q8NU77
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q8NU77
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.44 Å
R-Value Free: 0.259
R-Value Work: 0.209
R-Value Observed: 0.211
Space Group: C 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 104.097	α = 90
b = 40.69	β = 94.96
c = 89.938	γ = 90

Software Package:

Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
CrystalClear	data collection
HKL-2000	data reduction
CaspR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2011-06-01

Deposition Author(s):

Robertson, B.A.

Revision History (Full details and data files)

Version 1.0: 2011-06-01
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2017-11-08
Changes: Advisory, Refinement description
Version 1.3: 2018-01-24
Changes: Database references
Version 1.4: 2023-09-06
Changes: Advisory, 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 R01GM157729.