Phosphorus in PDB 1ads: An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications

Enzymatic activity of An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications

All present enzymatic activity of An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications:
1.1.1.21;

Protein crystallography data

The structure of An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications, PDB code: 1ads was solved by D.K.Wilson, F.A.Quiocho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.000, 67.120, 92.020, 90.00, 90.00, 90.00
R / Rfree (%) 20 / n/a

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications (pdb code 1ads). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 3 binding sites of Phosphorus where determined in the An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications, PDB code: 1ads:
Jump to Phosphorus binding site number: 1; 2; 3;

Phosphorus binding site 1 out of 3 in 1ads

Go back to Phosphorus Binding Sites List in 1ads
Phosphorus binding site 1 out of 3 in the An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P350

b:5.1
occ:1.00
 PA A:NAP350 0.0 5.1 1.0
O2A A:NAP350 1.4 7.3 1.0
O1A A:NAP350 1.5 5.0 1.0
O3 A:NAP350 1.6 7.1 1.0
O5B A:NAP350 1.6 5.4 1.0
C5B A:NAP350 2.7 3.4 1.0
PN A:NAP350 3.0 6.1 1.0
O5D A:NAP350 3.4 5.1 1.0
O1N A:NAP350 3.8 6.8 1.0
C5D A:NAP350 3.8 4.5 1.0
CA A:SER214 3.9 8.6 1.0
C4B A:NAP350 3.9 4.7 1.0
O2N A:NAP350 3.9 7.6 1.0
N A:SER214 3.9 7.3 1.0
CB A:LEU212 4.1 6.9 1.0
CA A:SER210 4.1 5.5 1.0
CD A:PRO211 4.2 4.7 1.0
N A:LEU212 4.2 6.6 1.0
N A:LYS262 4.2 3.7 1.0
CG A:LEU212 4.3 6.2 1.0
O4B A:NAP350 4.3 5.6 1.0
CD1 A:LEU212 4.4 6.6 1.0
C A:SER210 4.4 5.9 1.0
N A:PRO211 4.5 6.0 1.0
CB A:SER214 4.6 6.8 1.0
CA A:LEU212 4.7 7.3 1.0
CB A:LYS262 4.7 4.0 1.0
CD A:PRO215 4.8 10.3 1.0
CG A:PRO211 4.8 4.9 1.0
O A:LYS262 4.9 5.6 1.0
N A:SER210 4.9 5.0 1.0
N A:GLY213 4.9 6.8 1.0
OG A:SER214 4.9 9.3 1.0
C A:LEU212 4.9 8.1 1.0
CA A:PRO261 5.0 4.5 1.0

Phosphorus binding site 2 out of 3 in 1ads

Go back to Phosphorus Binding Sites List in 1ads
Phosphorus binding site 2 out of 3 in the An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P350

b:6.1
occ:1.00
 PN A:NAP350 0.0 6.1 1.0
O1N A:NAP350 1.5 6.8 1.0
O2N A:NAP350 1.5 7.6 1.0
O5D A:NAP350 1.6 5.1 1.0
O3 A:NAP350 1.6 7.1 1.0
C5D A:NAP350 2.7 4.5 1.0
PA A:NAP350 3.0 5.1 1.0
O2A A:NAP350 3.4 7.3 1.0
C3D A:NAP350 3.5 4.6 1.0
C4D A:NAP350 3.6 5.2 1.0
OG A:SER214 3.8 9.3 1.0
O1A A:NAP350 3.8 5.0 1.0
OG A:SER210 3.8 6.6 1.0
NZ A:LYS21 3.8 8.7 1.0
O3D A:NAP350 3.9 4.1 1.0
O5B A:NAP350 4.0 5.4 1.0
CA A:SER210 4.1 5.5 1.0
CE3 A:TRP20 4.1 10.1 1.0
CB A:SER214 4.1 6.8 1.0
C6N A:NAP350 4.2 7.3 1.0
O4D A:NAP350 4.2 5.5 1.0
C5B A:NAP350 4.3 3.4 1.0
N A:SER210 4.3 5.0 1.0
CE A:LYS21 4.4 10.7 1.0
CB A:LYS262 4.4 4.0 1.0
CB A:SER210 4.5 4.4 1.0
CA A:SER214 4.5 8.6 1.0
CZ3 A:TRP20 4.5 11.3 1.0
C2D A:NAP350 4.8 4.8 1.0
C5N A:NAP350 4.9 8.5 1.0
OD1 A:ASP216 4.9 14.2 1.0
C1D A:NAP350 5.0 5.5 1.0

Phosphorus binding site 3 out of 3 in 1ads

Go back to Phosphorus Binding Sites List in 1ads
Phosphorus binding site 3 out of 3 in the An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 3 of An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P350

b:8.8
occ:1.00
 P2B A:NAP350 0.0 8.8 1.0
O3X A:NAP350 1.5 10.3 1.0
O2X A:NAP350 1.5 11.2 1.0
O1X A:NAP350 1.5 6.1 1.0
O2B A:NAP350 1.6 8.8 1.0
C2B A:NAP350 2.7 5.5 1.0
NH1 A:ARG268 3.2 22.7 1.0
O A:HOH484 3.4 20.4 1.0
C3B A:NAP350 3.6 6.2 1.0
OG1 A:THR265 3.7 15.8 1.0
C1B A:NAP350 3.8 6.6 1.0
OG A:SER263 3.8 8.0 1.0
O3B A:NAP350 3.8 8.2 1.0
N A:VAL264 4.0 8.0 1.0
NZ A:LYS262 4.0 6.5 1.0
CA A:SER263 4.1 6.6 1.0
N9A A:NAP350 4.3 6.7 1.0
CG2 A:VAL264 4.3 8.1 1.0
CZ A:ARG268 4.4 22.1 1.0
CB A:SER263 4.4 5.5 1.0
CD A:ARG268 4.4 15.0 1.0
CB A:THR265 4.5 12.8 1.0
C A:SER263 4.6 5.9 1.0
N A:THR265 4.6 9.9 1.0
C8A A:NAP350 4.7 6.1 1.0
O A:LYS262 4.8 5.6 1.0
NE A:ARG268 4.9 19.1 1.0
C4B A:NAP350 4.9 4.7 1.0
CE A:LYS262 4.9 7.2 1.0
O4B A:NAP350 5.0 5.6 1.0

Reference:

D.K.Wilson, K.M.Bohren, K.H.Gabbay, F.A.Quiocho. An Unlikely Sugar Substrate Site in the 1.65 A Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications. Science V. 257 81 1992.
ISSN: ISSN 0036-8075
PubMed: 1621098
Page generated: Fri Sep 25 12:46:24 2020

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