6T26

X-ray crystal structure of Vibrio alkaline phosphatase with the non-competitive inhibitor cyclohexylamine

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.27 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.160 
  • R-Value Observed: 0.162 

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Literature

X-ray crystal structure of Vibrio alkaline phosphatase with the non-competitive inhibitor cyclohexylamine.

Asgeirsson, B., Markusson, S., Hlynsdottir, S.S., Helland, R., Hjorleifsson, J.G.

(2020) Biochem Biophys Rep 24: 100830-100830

  • DOI: https://doi.org/10.1016/j.bbrep.2020.100830
  • Primary Citation of Related Structures:  
    6T26

  • PubMed Abstract: 

    Para -nitrophenyl phosphate, the common substrate for alkaline phosphatase (AP), is available as a cyclohexylamine salt. Here, we report that cyclohexylamine is a non-competitive inhibitor of APs.

    • Organizational Affiliation: 

    Department of Biochemistry, Science Institute, University of Iceland, Dunhagi 3, 107 Reykjavik, Iceland.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Alkaline phosphatase
A, B
512Vibrio sp. G15-21Mutation(s): 0 
UniProt
Find proteins for Q93P54 (Vibrio sp. G15-21)
Explore Q93P54 
Go to UniProtKB:  Q93P54
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ93P54
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 5 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
HAI (Subject of Investigation/LOI)
Query on HAI
Download Ideal Coordinates CCD File 
J [auth A],
K [auth A],
U [auth B],
V [auth B]		CYCLOHEXYLAMMONIUM ION
C6 H14 N
PAFZNILMFXTMIY-UHFFFAOYSA-O
PO4
Query on PO4
Download Ideal Coordinates CCD File 
I [auth A],
T [auth B]		PHOSPHATE ION
O4 P
NBIIXXVUZAFLBC-UHFFFAOYSA-K
ZN
Query on ZN
Download Ideal Coordinates CCD File 
C [auth A],
D [auth A],
N [auth B],
O [auth B]		ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
CL
Query on CL
Download Ideal Coordinates CCD File 
F [auth A]
G [auth A]
H [auth A]
Q [auth B]
R [auth B]
F [auth A],
G [auth A],
H [auth A],
Q [auth B],
R [auth B],
S [auth B]
CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
MG
Query on MG
Download Ideal Coordinates CCD File 
E [auth A]
L [auth A]
M [auth A]
P [auth B]
W [auth B]
E [auth A],
L [auth A],
M [auth A],
P [auth B],
W [auth B],
X [auth B]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.27 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.160 
  • R-Value Observed: 0.162 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.916α = 90
b = 85.27β = 113.55
c = 84.785γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
Aimlessdata scaling
PDB_EXTRACTdata extraction
XDSdata reduction
PHASERphasing

Structure Validation

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Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
Other governmentIceland141619-051
Other governmentIceland196071-00911

Revision History  (Full details and data files)

  • Version 1.0: 2020-10-21
    Type: Initial release
  • Version 1.1: 2020-10-28
    Changes: Database references
  • Version 1.2: 2020-11-04
    Changes: Database references
  • Version 1.3: 2024-01-24
    Changes: Data collection, Database references, Refinement description