4V39

Deposited: 2014-10-17 Released: 2015-04-08
Deposition Author(s): Pavkov-Keller, T., Schmoelzer, K., Czabany, T., Luley-Goedl, C., Ribitsch, D., Schwab, H., Nidetzky, B., Gruber, K.

Experimental Data Snapshot

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

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

Literature

(2015) Chem Commun (Camb) 51: 3083

PubMed Abstract:
Structure-guided active-site redesign of a family GT-80 β-D-galactoside sialyltransferase (from Pasteurella dagmatis) to change enzyme regioselectivity from α-2,3 in the wild type to α-2,6 in a P7H-M117A double mutant is reported. Biochemical data for sialylation of lactose together with protein crystal structures demonstrate highly precise enzyme engineering.

Organizational Affiliation

Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010 Graz, Austria.

Macromolecule Content

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
SIALYLTRANSFERASE	A	388	Pasteurella dagmatis	Mutation(s): 2
UniProt
Find proteins for K9UUI6 (Pasteurella dagmatis) Explore K9UUI6 Go to UniProtKB: K9UUI6
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	K9UUI6
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Unit Cell:

Software Package:

Entry History

Deposition Author(s):

Pavkov-Keller, T.

Version 1.0: 2015-04-08
Type: Initial release
Version 1.1: 2017-09-27
Changes: Data collection
Version 1.2: 2024-01-10
Changes: Data collection, Database references, Other, Refinement description