5F4X

Fructose-1,6-bisphosphate aldolase K229M mutant from rabbit muscle

PDB DOI: https://doi.org/10.2210/pdb5F4X/pdb

Classification: LYASE
Organism(s): Oryctolagus cuniculus
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2015-12-03 Released: 2016-12-28
Deposition Author(s): LowKam, C., Arthus-Cartier, G.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.84 Å
R-Value Free: 0.174
R-Value Work: 0.146
R-Value Observed: 0.146

wwPDB Validation 3D Report Full Report

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

Literature

DECYCLIZATION DETERMINES DIASTEREOISOMERIC SUBSTRATE SPECIFICITY OF MAMMALIAN CLASS I FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE

LowKam, C., Arthus-Cartier, G., Sygusch, J.

To be published.

Macromolecule Content

Total Structure Weight: 157.25 kDa
Atom Count: 12,912
Modelled Residue Count: 1,452
Deposited Residue Count: 1,452
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Fructose-bisphosphate aldolase A	A, B, C, D	363	Oryctolagus cuniculus	Mutation(s): 1 Gene Names: ALDOA EC: 4.1.2.13
UniProt
Find proteins for P00883 (Oryctolagus cuniculus) Explore P00883 Go to UniProtKB: P00883
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P00883
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
GOL Query on GOL Download Ideal Coordinates CCD File SDF format, chain E [auth B] SDF format, chain F [auth D] MOL2 format, chain E [auth B] MOL2 format, chain F [auth D]	E [auth B], F [auth D]	GLYCEROL C₃ H₈ O₃ PEDCQBHIVMGVHV-UHFFFAOYSA-N		Interactions Focus chain E [auth B] Focus chain F [auth D] Interactions & Density Focus chain E [auth B] Focus chain F [auth D]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.84 Å
R-Value Free: 0.174
R-Value Work: 0.146
R-Value Observed: 0.146
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 83.477	α = 90
b = 103.194	β = 98.66
c = 84.527	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
HKL-2000	data reduction
HKL-2000	data scaling
PHENIX	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2016-12-28

Deposition Author(s):

Arthus-Cartier, G.

Revision History (Full details and data files)

Version 1.0: 2016-12-28
Type: Initial release
Version 1.1: 2023-09-27
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.