5ZMU

Crystal structure of a cis-epoxysuccinate hydrolase producing D(-)-tartaric acids

PDB DOI: https://doi.org/10.2210/pdb5ZMU/pdb

Classification: HYDROLASE
Organism(s): Bordetella sp. BK-52
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2018-04-06 Released: 2018-08-08
Deposition Author(s): Dong, S., Liu, X., Wang, X., Feng, Y.
Funding Organization(s): National Natural Science Foundation of China

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.50 Å
R-Value Free: 0.170
R-Value Work: 0.149
R-Value Observed: 0.149

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

Structural insight into the catalytic mechanism of a cis-epoxysuccinate hydrolase producing enantiomerically pure d(-)-tartaric acid.

Dong, S., Liu, X., Cui, G.Z., Cui, Q., Wang, X., Feng, Y.

(2018) Chem Commun (Camb) 54: 8482-8485

PubMed: 30003205 Search on PubMed
DOI: https://doi.org/10.1039/c8cc04398a
Primary Citation of Related Structures:
5ZMU, 5ZMY

PubMed Abstract:
Crystal structure determination and mutagenesis analysis of a cis-epoxysuccinate hydrolase which produces enantiomerically pure d(-)-tartaric acids revealed a zinc ion and essential residues in the stereoselective mechanism for the catalytic reaction of the small mirror symmetric substrate.

Organizational Affiliation

Shandong Provincial Key Laboratory of Synthetic Biology and CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Songling Road 189, Qingdao, Shandong 266101, China. [email protected] [email protected].

Macromolecule Content

Total Structure Weight: 139.03 kDa
Atom Count: 10,515
Modelled Residue Count: 1,129
Deposited Residue Count: 1,256
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Cis-epoxysuccinate hydrolase	A, B, C, D	314	Bordetella sp. BK-52	Mutation(s): 0
UniProt
Find proteins for F1LJ99 (Bordetella sp. BK-52) Explore F1LJ99 Go to UniProtKB: F1LJ99
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	F1LJ99
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ZN Query on ZN Download Ideal Coordinates CCD File SDF format, chain E [auth A] SDF format, chain F [auth B] SDF format, chain G [auth C] SDF format, chain H [auth D] MOL2 format, chain E [auth A] MOL2 format, chain F [auth B] MOL2 format, chain G [auth C] MOL2 format, chain H [auth D] mmCIF format, chain E [auth A] mmCIF format, chain F [auth B] mmCIF format, chain G [auth C] mmCIF format, chain H [auth D]	E [auth A], F [auth B], G [auth C], H [auth D]	ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N		Interactions Focus chain E [auth A] Focus chain F [auth B] Focus chain G [auth C] Focus chain H [auth D] Interactions & Density Focus chain E [auth A] Focus chain F [auth B] Focus chain G [auth C] Focus chain H [auth D]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.50 Å
R-Value Free: 0.170
R-Value Work: 0.149
R-Value Observed: 0.149
Space Group: P 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 78.49	α = 90
b = 94.25	β = 95.898
c = 94.36	γ = 90

Software Package:

Software Name	Purpose
phenix.refine	refinement
PHENIX	refinement
XDS	data reduction
XDS	data scaling
PHASER	phasing
ARP/wARP	model building

Structure Validation

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Entry History & Funding Information

Deposition Data

Released Date: 2018-08-08

Deposition Author(s):

Funding Organization	Location	Grant Number
National Natural Science Foundation of China	China	31670735

Revision History (Full details and data files)

Version 1.0: 2018-08-08
Type: Initial release
Version 1.1: 2023-11-22
Changes: Data collection, Database references, Derived calculations, Refinement description