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Arsenic in PDB 2x2p: The Flavoprotein Nrdi From Bacillus Cereus with the Initially Semiquinone Fmn Cofactor in An Intermediate Radiation Reduced State

Protein crystallography data

The structure of The Flavoprotein Nrdi From Bacillus Cereus with the Initially Semiquinone Fmn Cofactor in An Intermediate Radiation Reduced State, PDB code: 2x2p was solved by A.K.Rohr, H.P.Hersleth, K.K.Andersson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.955, 45.485, 56.200, 90.00, 90.00, 90.00
R / Rfree (%) n/a / 19.1

Other elements in 2x2p:

The structure of The Flavoprotein Nrdi From Bacillus Cereus with the Initially Semiquinone Fmn Cofactor in An Intermediate Radiation Reduced State also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the The Flavoprotein Nrdi From Bacillus Cereus with the Initially Semiquinone Fmn Cofactor in An Intermediate Radiation Reduced State (pdb code 2x2p). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the The Flavoprotein Nrdi From Bacillus Cereus with the Initially Semiquinone Fmn Cofactor in An Intermediate Radiation Reduced State, PDB code: 2x2p:

Arsenic binding site 1 out of 1 in 2x2p

Go back to Arsenic Binding Sites List in 2x2p
Arsenic binding site 1 out of 1 in the The Flavoprotein Nrdi From Bacillus Cereus with the Initially Semiquinone Fmn Cofactor in An Intermediate Radiation Reduced State


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of The Flavoprotein Nrdi From Bacillus Cereus with the Initially Semiquinone Fmn Cofactor in An Intermediate Radiation Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As1124

b:12.0
occ:0.85
AS A:CAC1124 0.0 12.0 0.8
O1 A:CAC1124 1.6 14.8 0.8
O2 A:CAC1124 1.7 9.0 0.8
C1 A:CAC1124 1.9 16.2 0.8
C2 A:CAC1124 1.9 16.1 0.8
ZN A:ZN1120 3.2 9.3 1.0
OH A:TYR5 3.7 10.9 1.0
O A:HOH2016 3.8 25.4 1.0
O A:HOH2137 3.9 17.0 1.0
O A:HOH2138 4.1 40.5 1.0
NE2 A:HIS17 4.1 8.5 1.0
CE1 A:HIS17 4.3 9.1 1.0
O A:HOH2033 4.6 27.8 1.0
CZ A:TYR5 4.7 9.0 1.0
O A:HOH2129 4.8 18.4 1.0
CE1 A:TYR5 4.8 8.2 1.0
CD1 A:ILE16 5.0 9.0 0.5
O A:HOH2017 5.0 20.5 1.0

Reference:

A.K.Rohr, H.P.Hersleth, K.K.Andersson. Tracking Flavin Conformations in Protein Crystal Structures with Raman Spectroscopy and Qm/Mm Calculations Angew.Chem.Int.Ed.Engl. V. 49 2324 2010.
ISSN: ISSN 1433-7851
PubMed: 20187055
DOI: 10.1002/ANIE.200907143
Page generated: Sun Jul 6 23:17:30 2025

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