6AG8

Crystal structure of Maltose O-acetyltransferase from E. coli

PDB DOI: https://doi.org/10.2210/pdb6AG8/pdb

Classification: TRANSFERASE
Organism(s): Escherichia coli K-12
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2018-08-09 Released: 2019-08-28
Deposition Author(s): Joo, S., Kim, K.-J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.34 Å
R-Value Free: 0.190
R-Value Work: 0.171
R-Value Observed: 0.172

wwPDB Validation 3D Report Full Report

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

Literature

Metabolic engineering of Escherichia coli for production of non-natural acetins from glycerol

Zada, B., Joo, S., Wang, C., Kim, K.-J., Kim, S.-W.

To be published.

Macromolecule Content

Total Structure Weight: 42.62 kDa
Atom Count: 3,119
Modelled Residue Count: 364
Deposited Residue Count: 382
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Maltose O-acetyltransferase	A [auth C], B [auth A]	191	Escherichia coli K-12	Mutation(s): 0 Gene Names: maa, ylaD, b0459, JW0448 EC: 2.3.1.79
UniProt
Find proteins for P77791 (Escherichia coli (strain K12)) Explore P77791 Go to UniProtKB: P77791
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P77791
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
TRS Query on TRS Download Ideal Coordinates CCD File SDF format, chain C SDF format, chain D [auth A] MOL2 format, chain C MOL2 format, chain D [auth A]	C, D [auth A]	2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL C₄ H₁₂ N O₃ LENZDBCJOHFCAS-UHFFFAOYSA-O		Interactions Focus chain C Focus chain D [auth A] Interactions & Density Focus chain C Focus chain D [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.34 Å
R-Value Free: 0.190
R-Value Work: 0.171
R-Value Observed: 0.172
Space Group: P 3

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 62.104	α = 90
b = 62.104	β = 90
c = 81.128	γ = 120

Software Package:

Software Name	Purpose
REFMAC	refinement
HKL-2000	data scaling
MOLREP	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2019-08-28

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2019-08-28
Type: Initial release
Version 1.1: 2023-11-22
Changes: Data collection, Database references, Refinement description

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.