1QO7

Structure of Aspergillus niger epoxide hydrolase

PDB DOI: https://doi.org/10.2210/pdb1QO7/pdb

Classification: HYDROLASE
Organism(s): Aspergillus niger
Expression System: Escherichia coli BL21(DE3)
Mutation(s): Yes

Deposited: 1999-11-04 Released: 2000-02-10
Deposition Author(s): Zou, J.-Y., Hallberg, B.M., Bergfors, T., Oesch, F., Arand, M., Mowbray, S.L., Jones, T.A.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.80 Å
R-Value Free: 0.232
R-Value Work: 0.224
R-Value Observed: 0.224

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Structure of Aspergillus Niger Epoxide Hydrolase at 1.8A Resolution: Implications for the Structure and Function of the Mammalian Microsomal Class of Epoxide Hydrolases

Zou, J.-Y., Hallberg, B.M., Bergfors, T., Oesch, F., Arand, M., Mowbray, S.L., Jones, T.A.

(2000) Structure 8: 111

PubMed: 10673439 Search on PubMed
DOI: https://doi.org/10.1016/s0969-2126(00)00087-3
Primary Citation of Related Structures:
1QO7

PubMed Abstract:
Epoxide hydrolases have important roles in the defense of cells against potentially harmful epoxides. Conversion of epoxides into less toxic and more easily excreted diols is a universally successful strategy. A number of microorganisms employ the same chemistry to process epoxides for use as carbon sources.

Organizational Affiliation

Department of Cell and Molecular Biology, BMC, Uppsala University, Box 596, Uppsala, S-751 24, Sweden.

Macromolecule Content

Total Structure Weight: 88.25 kDa
Atom Count: 6,502
Modelled Residue Count: 770
Deposited Residue Count: 788
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
EPOXIDE HYDROLASE	A, B	394	Aspergillus niger	Mutation(s): 2 EC: 3.3.2.3
UniProt
Find proteins for Q9UR30 (Aspergillus niger) Explore Q9UR30 Go to UniProtKB: Q9UR30
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9UR30
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.80 Å
R-Value Free: 0.232
R-Value Work: 0.224
R-Value Observed: 0.224
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 62.69	α = 90
b = 89.32	β = 105.37
c = 75.77	γ = 90

Software Package:

Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
CNS	phasing
SOLVE	phasing
CNS	refinement

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2000-02-10

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2000-02-10
Type: Initial release
Version 1.1: 2011-05-08
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.