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Arsenic in PDB 2acr: An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate

Enzymatic activity of An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate

All present enzymatic activity of An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate:
1.1.1.21;

Protein crystallography data

The structure of An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate, PDB code: 2acr was solved by D.H.Harrison, K.M.Bohren, K.H.Gabbay, G.A.Petsko, D.Ringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.76
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.110, 67.200, 92.180, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / n/a

Arsenic Binding Sites:

The binding sites of Arsenic atom in the An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate (pdb code 2acr). 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 An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate, PDB code: 2acr:

Arsenic binding site 1 out of 1 in 2acr

Go back to Arsenic Binding Sites List in 2acr
Arsenic binding site 1 out of 1 in the An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As317

b:48.8
occ:1.00
 AS A:CAC317 0.0 48.8 1.0
O2 A:CAC317 1.8 38.0 1.0
O1 A:CAC317 1.8 39.5 1.0
C2 A:CAC317 2.0 41.6 1.0
C1 A:CAC317 2.0 40.8 1.0
O A:HOH322 3.8 26.5 1.0
CE1 A:HIS110 3.8 5.8 1.0
C4N A:NAP316 3.9 4.9 1.0
O7N A:NAP316 4.0 7.9 1.0
CE1 A:TYR48 4.0 5.4 1.0
O A:HOH346 4.0 41.4 1.0
O A:HOH345 4.1 49.6 1.0
NE2 A:HIS110 4.2 8.7 1.0
C3N A:NAP316 4.4 2.2 1.0
OH A:TYR48 4.4 5.0 1.0
CE2 A:TRP20 4.4 5.4 1.0
C7N A:NAP316 4.5 6.9 1.0
CD2 A:TRP20 4.5 4.4 1.0
C5N A:NAP316 4.6 2.8 1.0
NE1 A:TRP20 4.7 4.7 1.0
NE1 A:TRP111 4.7 5.0 1.0
CZ A:TYR48 4.7 4.6 1.0
CZ2 A:TRP20 4.8 5.3 1.0
CG A:TRP20 4.8 5.1 1.0
O A:HOH323 4.8 41.7 1.0
CD1 A:TRP20 4.8 5.4 1.0
CE3 A:TRP20 4.9 4.1 1.0
ND1 A:HIS110 4.9 8.2 1.0

Reference:

D.H.Harrison, K.M.Bohren, D.Ringe, G.A.Petsko, K.H.Gabbay. An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose 6-Phosphate. Biochemistry V. 33 2011 1994.
ISSN: ISSN 0006-2960
PubMed: 8117658
DOI: 10.1021/BI00174A006
Page generated: Wed Jul 10 11:18:34 2024

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