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Chlorine in PDB 8fh7: Crystal Structure of Aldose Reductase (AKR1B1) Complexed with Nadp+ and at-003

Enzymatic activity of Crystal Structure of Aldose Reductase (AKR1B1) Complexed with Nadp+ and at-003

All present enzymatic activity of Crystal Structure of Aldose Reductase (AKR1B1) Complexed with Nadp+ and at-003:
1.1.1.21; 1.1.1.300; 1.1.1.372; 1.1.1.54;

Protein crystallography data

The structure of Crystal Structure of Aldose Reductase (AKR1B1) Complexed with Nadp+ and at-003, PDB code: 8fh7 was solved by R.Arenas, D.K.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.73 / 1.45
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 40.186, 46.957, 47.379, 75.77, 67.47, 76.87
R / Rfree (%) 14.5 / 16.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Aldose Reductase (AKR1B1) Complexed with Nadp+ and at-003 (pdb code 8fh7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Aldose Reductase (AKR1B1) Complexed with Nadp+ and at-003, PDB code: 8fh7:

Chlorine binding site 1 out of 1 in 8fh7

Go back to Chlorine Binding Sites List in 8fh7
Chlorine binding site 1 out of 1 in the Crystal Structure of Aldose Reductase (AKR1B1) Complexed with Nadp+ and at-003


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Aldose Reductase (AKR1B1) Complexed with Nadp+ and at-003 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:19.8
occ:1.00
CL19 A:XY0402 0.0 19.8 1.0
C15 A:XY0402 1.7 16.5 1.0
C16 A:XY0402 2.6 18.3 1.0
C14 A:XY0402 2.7 16.7 1.0
H16 A:XY0402 2.7 17.4 1.0
H14 A:XY0402 2.8 16.2 1.0
HD1 A:TYR309 2.9 15.8 1.0
HG21 A:THR113 3.0 11.1 1.0
HB3 A:CYS303 3.1 22.7 1.0
HD2 A:PRO310 3.2 11.8 1.0
HB2 A:CYS303 3.4 22.7 1.0
HG22 A:THR113 3.4 11.1 1.0
HE3 A:TRP111 3.5 10.5 1.0
HD3 A:PRO310 3.5 11.8 1.0
HG A:CYS303 3.6 28.2 0.0
CD1 A:TYR309 3.6 15.9 1.0
CG2 A:THR113 3.6 10.9 1.0
CB A:CYS303 3.7 21.6 1.0
HG1 A:THR113 3.7 12.1 0.0
HE1 A:TYR309 3.7 16.4 1.0
HA A:TYR309 3.7 13.6 1.0
OG1 A:THR113 3.7 12.1 1.0
CD A:PRO310 3.8 11.9 1.0
CE3 A:TRP111 3.8 9.9 1.0
C12 A:XY0402 3.9 16.2 1.0
C13 A:XY0402 3.9 14.8 1.0
CE1 A:TYR309 4.0 16.1 1.0
HZ3 A:TRP111 4.1 11.4 1.0
CZ3 A:TRP111 4.2 12.2 1.0
HB3 A:TRP111 4.2 9.2 1.0
CB A:THR113 4.3 11.6 1.0
SG A:CYS303 4.4 28.2 1.0
C11 A:XY0402 4.4 15.8 1.0
HG23 A:THR113 4.4 11.1 1.0
HG3 A:PRO310 4.5 11.0 1.0
CD2 A:TRP111 4.5 10.6 1.0
CG A:PRO310 4.6 10.7 1.0
CG A:TYR309 4.7 15.0 1.0
CA A:TYR309 4.7 13.5 1.0
H13 A:XY0402 4.7 15.5 1.0
HB A:THR113 4.7 11.4 1.0
HZ A:PHE115 4.7 11.1 1.0
HG2 A:PRO310 4.8 11.0 1.0
O A:CYS303 4.8 19.5 1.0
HE1 A:PHE115 4.8 11.5 1.0
HD2 A:PRO112 4.9 8.9 1.0
HB2 A:TYR309 4.9 13.9 1.0
H A:LEU300 4.9 25.7 1.0
CB A:TYR309 5.0 13.7 1.0

Reference:

R.Arenas, D.K.Wilson. Crystal Structure of Aldose Reductase (AKR1B1) Complexed with Nadp+ and at-003 To Be Published.
Page generated: Thu Dec 28 03:12:38 2023

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