5NUX

Thermus scotoductus SA-01 Ene-reductase double mutant TsER_C25D_I67T

PDB DOI: https://doi.org/10.2210/pdb5NUX/pdb

Classification: OXIDOREDUCTASE
Organism(s): Thermus scotoductus
Expression System: Escherichia coli BL21(DE3)
Mutation(s): Yes

Deposited: 2017-05-03 Released: 2018-05-30
Deposition Author(s): Opperman, D.J., Hoebenreich, S., Nett, N.
Funding Organization(s): State of Hesse

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.223
R-Value Work: 0.182
R-Value Observed: 0.184

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

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

Literature

A robust and stereocomplementary panel of ene-reductase variants for gram-scale asymmetric hydrogenation

Nett, N., Duewel, S., Schmermund, L., Benary, G.E., Ranaghan, K., Mulholland, A., Opperman, D.J., Hoebenreich, S.

(2021) Mol Catal 502: 111404

DOI: https://doi.org/10.1016/j.mcat.2021.111404

Macromolecule Content

Total Structure Weight: 153.93 kDa
Atom Count: 11,185
Modelled Residue Count: 1,392
Deposited Residue Count: 1,396
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Chromate reductase	A, B, C, D	349	Thermus scotoductus	Mutation(s): 2 Gene Names: chrR
UniProt
Find proteins for B0JDW3 (Thermus scotoductus) Explore B0JDW3 Go to UniProtKB: B0JDW3
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	B0JDW3
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FMN Query on FMN 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]	FLAVIN MONONUCLEOTIDE C₁₇ H₂₁ N₄ O₉ P FVTCRASFADXXNN-SCRDCRAPSA-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: 2.30 Å
R-Value Free: 0.223
R-Value Work: 0.182
R-Value Observed: 0.184
Space Group: P 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 99.68	α = 90
b = 101.2	β = 115.24
c = 104.26	γ = 90

Software Package:

Software Name	Purpose
SCALA	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
MOSFLM	data reduction

Structure Validation

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Ligand Structure Quality Assessment

Entry History & Funding Information

Deposition Data

Released Date: 2018-05-30

Deposition Author(s):

Opperman, D.J.

Hoebenreich, S.

Nett, N.

Funding Organization	Location	Grant Number
State of Hesse	Germany	LOEWE research cluster SynChemBio

Revision History (Full details and data files)

Version 1.0: 2018-05-30
Type: Initial release
Version 1.1: 2022-02-16
Changes: Database references
Version 1.2: 2024-01-17
Changes: Data collection, Database references, Refinement description

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5NUX

Thermus scotoductus SA-01 Ene-reductase double mutant TsER_C25D_I67T

A robust and stereocomplementary panel of ene-reductase variants for gram-scale asymmetric hydrogenation

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)