3PK2

Artificial Transfer Hydrogenases for the Enantioselective Reduction of Cyclic Imines

PDB DOI: https://doi.org/10.2210/pdb3PK2/pdb

Classification: BIOTIN-BINDING PROTEIN
Organism(s): Streptomyces avidinii
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2010-11-11 Released: 2011-04-13
Deposition Author(s): Schirmer, T., Heinisch, T.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.90 ?
R-Value Free: 0.204
R-Value Work: 0.184
R-Value Observed: 0.185

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

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines.

Durrenberger, M., Heinisch, T., Wilson, Y.M., Rossel, T., Nogueira, E., Knorr, L., Mutschler, A., Kersten, K., Zimbron, M.J., Pierron, J., Schirmer, T., Ward, T.R.

(2011) Angew Chem Int Ed Engl 50: 3026-3029

PubMed: 21404391 Search on PubMed
DOI: https://doi.org/10.1002/anie.201007820
Primary Citation of Related Structures:
3PK2

Organizational Affiliation

Institut für Anorganische Chemie, Universit?t Basel, Basel, Switzerland.

Macromolecule Content

Total Structure Weight: 17.75 kDa
Atom Count: 1,033
Modelled Residue Count: 122
Deposited Residue Count: 159
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Streptavidin	A	159	Streptomyces avidinii	Mutation(s): 1
UniProt
Find proteins for P22629 (Streptomyces avidinii) Explore P22629 Go to UniProtKB: P22629
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P22629
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
4IR Query on 4IR Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A] mmCIF format, chain B [auth A]	B [auth A]	{N-(4-{[2-(amino-kappaN)ethyl]sulfamoyl-kappaN}phenyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide}(chloro)[(1,2,3,4,5-eta)-1,2,3,4,5-pentamethylcyclopentadienyl]iridium(III) C₂₈ H₄₅ Cl Ir N₅ O₄ S₂ OPJZDGOSRZOXTM-DYKJULMGSA-M		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]
IR3 Query on IR3 Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth A] MOL2 format, chain C [auth A] MOL2 format, chain D [auth A] mmCIF format, chain C [auth A] mmCIF format, chain D [auth A]	C [auth A], D [auth A]	IRIDIUM (III) ION Ir MILUBEOXRNEUHS-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Focus chain D [auth A] Interactions & Density Focus chain C [auth A] Focus chain D [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.90 ?
R-Value Free: 0.204
R-Value Work: 0.184
R-Value Observed: 0.185
Space Group: I 4₁ 2 2

Unit Cell:

Length ( ? )	Angle ( ? )
a = 57.616	α = 90
b = 57.616	β = 90
c = 184.031	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
MOSFLM	data reduction
SCALA	data scaling

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2011-04-13

Deposition Author(s):

Schirmer, T.

Heinisch, T.

Revision History (Full details and data files)

Version 1.0: 2011-04-13
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2023-09-06
Changes: Data collection, Database references, Derived calculations, Refinement description

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3PK2

Artificial Transfer Hydrogenases for the Enantioselective Reduction of Cyclic Imines

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines.

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)