5DX6

Acetolactate Synthase from Klebsiella pneumoniae soaked with beta-fluoropyruvate


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.190 
  • R-Value Work: 0.151 
  • R-Value Observed: 0.152 

Starting Model: experimental
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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Characterization of Acetolactate Synthase from Klebsiella pneumoniae

Latta, A.J.McLeish, M.J.Andrews, F.H.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Acetolactate synthase, catabolic
A, B
579Klebsiella pneumoniaeMutation(s): 0 
Gene Names: budBilvK
EC: 2.2.1.6
UniProt
Find proteins for P27696 (Klebsiella pneumoniae)
Explore P27696 
Go to UniProtKB:  P27696
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP27696
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 5 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
5GY
Query on 5GY

Download Ideal Coordinates CCD File 
F [auth A]3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-[(1R)-2-fluoro-1-hydroxyethyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium
C14 H22 F N4 O8 P2 S
RCUDZGRKYWDHTO-LLVKDONJSA-O
TPP
Query on TPP

Download Ideal Coordinates CCD File 
I [auth B]THIAMINE DIPHOSPHATE
C12 H19 N4 O7 P2 S
AYEKOFBPNLCAJY-UHFFFAOYSA-O
65S
Query on 65S

Download Ideal Coordinates CCD File 
J [auth B]3-fluoro-2-oxopropanoic acid
C3 H3 F O3
CXABZTLXNODUTD-UHFFFAOYSA-N
PO4
Query on PO4

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C [auth A]PHOSPHATE ION
O4 P
NBIIXXVUZAFLBC-UHFFFAOYSA-K
MG
Query on MG

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D [auth A],
E [auth A],
G [auth B],
H [auth B]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.190 
  • R-Value Work: 0.151 
  • R-Value Observed: 0.152 
  • Space Group: I 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 84.8α = 90
b = 134.01β = 95.5
c = 110.772γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
MOSFLMdata reduction
Aimlessdata scaling
PHASERphasing
PDB_EXTRACTdata extraction

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Science Foundation (NSF, United States)United States--

Revision History  (Full details and data files)

  • Version 1.0: 2016-09-28
    Type: Initial release
  • Version 1.1: 2017-09-20
    Changes: Author supporting evidence, Derived calculations
  • Version 1.2: 2019-11-27
    Changes: Author supporting evidence
  • Version 1.3: 2023-09-27
    Changes: Data collection, Database references, Derived calculations, Refinement description