1DW9

Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.189 
  • R-Value Work: 0.150 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Structure of Cyanase Reveals that a Novel Dimeric and Decameric Arrangement of Subunits is Required for Formation of the Enzyme Active Site

Walsh, M.A., Otwinowski, Z., Perrakis, A., Anderson, P.M., Joachimiak, A.

(2000) Structure 8: 505

  • DOI: https://doi.org/10.1016/s0969-2126(00)00134-9
  • Primary Citation of Related Structures:  
    1DW9, 1DWK

  • PubMed Abstract: 

    Cyanase is an enzyme found in bacteria and plants that catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. In Escherichia coli, cyanase is induced from the cyn operon in response to extracellular cyanate. The enzyme is functionally active as a homodecamer of 17 kDa subunits, and displays half-site binding of substrates or substrate analogs. The enzyme shows no significant amino acid sequence homology with other proteins.

    • Organizational Affiliation: 

    Biosciences Division/Structural Biology Center, Argonne National Laboratory, Argonne, IL 60439, USA.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CYANATE LYASE
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J
156Escherichia coliMutation(s): 0 
EC: 4.3.99.1
UniProt
Find proteins for P00816 (Escherichia coli (strain K12))
Explore P00816 
Go to UniProtKB:  P00816
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00816
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4
Download Ideal Coordinates CCD File 
BA [auth F]
CA [auth F]
EA [auth G]
FA [auth G]
HA [auth H]
BA [auth F],
CA [auth F],
EA [auth G],
FA [auth G],
HA [auth H],
IA [auth H],
JA [auth H],
L [auth A],
LA [auth I],
M [auth A],
MA [auth I],
O [auth B],
OA [auth J],
P [auth B],
PA [auth J],
QA [auth J],
R [auth C],
T [auth D],
U [auth D],
V [auth D],
X [auth E],
Y [auth E],
Z [auth E]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
CL
Query on CL
Download Ideal Coordinates CCD File 
AA [auth F]
DA [auth G]
GA [auth H]
K [auth A]
KA [auth I]
AA [auth F],
DA [auth G],
GA [auth H],
K [auth A],
KA [auth I],
N [auth B],
NA [auth J],
Q [auth C],
S [auth D],
W [auth E]
CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.189 
  • R-Value Work: 0.150 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.34α = 70.3
b = 81.03β = 72.2
c = 82.3γ = 66.4
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-05-16
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Atomic model, Version format compliance
  • Version 1.2: 2011-09-28
    Changes: Atomic model, Derived calculations, Non-polymer description, Other, Refinement description
  • Version 1.3: 2019-05-08
    Changes: Data collection, Derived calculations, Experimental preparation, Other
  • Version 1.4: 2019-08-21
    Changes: Data collection, Database references