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Bromine in PDB 2r24: Human Aldose Reductase Structure

Enzymatic activity of Human Aldose Reductase Structure

All present enzymatic activity of Human Aldose Reductase Structure:
1.1.1.21;

Protein crystallography data

The structure of Human Aldose Reductase Structure, PDB code: 2r24 was solved by M.P.Blakeley, F.Ruiz, R.Cachau, I.Hazemann, F.Meilleur, A.Mitschler, S.Ginell, P.Afonine, O.N.Ventura, A.Cousido-Siah, M.Haertlein, A.Joachimiak, D.Myles, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 50.066, 67.126, 47.862, 90.00, 92.41, 90.00
R / Rfree (%) 25.7 / 29.1

Other elements in 2r24:

The structure of Human Aldose Reductase Structure also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Human Aldose Reductase Structure (pdb code 2r24). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Human Aldose Reductase Structure, PDB code: 2r24:

Bromine binding site 1 out of 1 in 2r24

Go back to Bromine Binding Sites List in 2r24
Bromine binding site 1 out of 1 in the Human Aldose Reductase Structure


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Human Aldose Reductase Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br317

b:18.8
occ:1.00
BR8 A:LDT317 0.0 18.8 1.0
C25 A:LDT317 1.9 10.4 1.0
DG1 A:THR113 2.4 14.2 1.0
C28 A:LDT317 2.9 10.2 1.0
C29 A:LDT317 2.9 10.1 1.0
OG1 A:THR113 2.9 13.6 1.0
DB3 A:TRP111 3.3 3.7 1.0
DZ A:PHE115 3.4 4.0 1.0
DG A:CYS80 3.4 13.7 1.0
DB3 A:CYS303 3.5 26.3 1.0
DG21 A:THR113 3.6 7.1 1.0
DG A:CYS303 3.7 28.4 1.0
DD1 A:TYR309 3.8 17.6 1.0
DE3 A:TRP111 3.8 6.6 1.0
CE3 A:TRP111 3.9 5.7 1.0
CD2 A:TRP111 3.9 5.4 1.0
DE1 A:PHE115 3.9 10.2 1.0
CB A:TRP111 4.0 4.7 1.0
CG A:TRP111 4.0 5.2 1.0
SG A:CYS303 4.0 27.2 1.0
DG23 A:THR113 4.0 12.4 1.0
DB2 A:TRP111 4.0 3.1 1.0
CB A:CYS303 4.0 23.2 1.0
CB A:THR113 4.1 10.8 1.0
CG2 A:THR113 4.1 8.6 1.0
CZ A:PHE115 4.1 8.2 1.0
DB2 A:CYS303 4.1 20.7 1.0
DE1 A:TYR309 4.2 29.6 1.0
C27 A:LDT317 4.2 12.3 1.0
C26 A:LDT317 4.2 13.3 1.0
CE1 A:PHE115 4.4 10.0 1.0
DB A:THR113 4.4 12.6 1.0
D A:THR113 4.5 10.8 1.0
CD1 A:TYR309 4.5 21.2 1.0
CZ3 A:TRP111 4.7 6.2 1.0
CE1 A:TYR309 4.7 23.6 1.0
SG A:CYS80 4.7 8.8 1.0
CE2 A:TRP111 4.7 7.7 1.0
DD2 A:PRO310 4.7 9.6 1.0
C24 A:LDT317 4.7 12.4 1.0
CD1 A:TRP111 4.7 7.9 1.0
DD3 A:PRO310 4.8 10.6 1.0
DD23 A:LEU300 4.9 21.4 1.0
DZ3 A:TRP111 5.0 3.6 1.0

Reference:

M.P.Blakeley, F.Ruiz, R.Cachau, I.Hazemann, F.Meilleur, A.Mitschler, S.Ginell, P.Afonine, O.N.Ventura, A.Cousido-Siah, M.Haertlein, A.Joachimiak, D.Myles, A.Podjarny. Quantum Model of Catalysis Based on Mobile Proton Revealed By Subatomic X-Ray and Neutron Diffraction Studies of H-Aldose Reductase Proc.Natl.Acad.Sci.Usa V. 105 1844 2008.
ISSN: ISSN 0027-8424
PubMed: 18250329
DOI: 10.1073/PNAS.0711659105
Page generated: Sat Dec 12 02:08:09 2020

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