3ZGJ

S221M V223F Y359A mutant of 4-Hydroxymandelate synthase from Streptomyces coelicolor

PDB DOI: https://doi.org/10.2210/pdb3ZGJ/pdb

Classification: OXIDOREDUCTASE
Organism(s): Streptomyces coelicolor A3(2)
Expression System: Escherichia coli BL21(DE3)
Mutation(s): Yes

Deposited: 2012-12-18 Released: 2013-10-30
Deposition Author(s): Pratter, S., Straganz, G., Grogan, G.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.95 Å
R-Value Free: 0.215
R-Value Work: 0.175
R-Value Observed: 0.177

Starting Model: experimental
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This is version 1.2 of the entry. See complete history.

Literature

Inversion of Enantioselectivity of a Mononuclear Non-Heme Iron(II)-Dependent Hydroxylase by Tuning the Interplay of Metal Center Geometry and Protein Structure

Pratter, S., Konstantinovics, C., Digiuro, C.L.M., Leitner, E., Kumar, D., De Visser, S.P., Grogan, G., Straganz, G.

(2013) Angew Chem Int Ed Engl 52: 9677

PubMed: 23881738 Search on PubMed
DOI: https://doi.org/10.1002/anie.201304633
Primary Citation of Related Structures:
3ZGJ

Organizational Affiliation

Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12, 8010 Graz, Austria.

Macromolecule Content

Total Structure Weight: 80.9 kDa
Atom Count: 5,614
Modelled Residue Count: 670
Deposited Residue Count: 742
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
4-HYDROXYPHENYLPYRUVIC ACID DIOXYGENASE	A, B	371	Streptomyces coelicolor A3(2)	Mutation(s): 3 EC: 1.13.11.46
UniProt
Find proteins for Q9Z4X7 (Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)) Explore Q9Z4X7 Go to UniProtKB: Q9Z4X7
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9Z4X7
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
RMN Query on RMN Download Ideal Coordinates CCD File SDF format, chain D [auth A] SDF format, chain F [auth B] MOL2 format, chain D [auth A] MOL2 format, chain F [auth B] mmCIF format, chain D [auth A] mmCIF format, chain F [auth B]	D [auth A], F [auth B]	(R)-MANDELIC ACID C₈ H₈ O₃ IWYDHOAUDWTVEP-SSDOTTSWSA-N		Interactions Focus chain D [auth A] Focus chain F [auth B] Interactions & Density Focus chain D [auth A] Focus chain F [auth B]
CO Query on CO Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain E [auth B] MOL2 format, chain C [auth A] MOL2 format, chain E [auth B] mmCIF format, chain C [auth A] mmCIF format, chain E [auth B]	C [auth A], E [auth B]	COBALT (II) ION Co XLJKHNWPARRRJB-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Focus chain E [auth B] Interactions & Density Focus chain C [auth A] Focus chain E [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.95 Å
R-Value Free: 0.215
R-Value Work: 0.175
R-Value Observed: 0.177
Space Group: P 4

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 122.87	α = 90
b = 122.87	β = 90
c = 54.86	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
XDS	data reduction
SCALA	data scaling
MOLREP	phasing

Structure Validation

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Entry History

Deposition Data

Released Date: 2013-10-30

Deposition Author(s):

Pratter, S.

Straganz, G.

Grogan, G.

Revision History (Full details and data files)

Version 1.0: 2013-10-30
Type: Initial release
Version 1.1: 2023-12-20
Changes: Data collection, Database references, Derived calculations, Other, Refinement description
Version 1.2: 2024-10-23
Changes: Structure summary

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Help and Resources

3ZGJ

S221M V223F Y359A mutant of 4-Hydroxymandelate synthase from Streptomyces coelicolor

Inversion of Enantioselectivity of a Mononuclear Non-Heme Iron(II)-Dependent Hydroxylase by Tuning the Interplay of Metal Center Geometry and Protein Structure

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

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Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)