Atomistry » Potassium » PDB 1d7v-1gmk » 1ehy
Atomistry »
  Potassium »
    PDB 1d7v-1gmk »
      1ehy »

Potassium in PDB 1ehy: X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1

Enzymatic activity of X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1

All present enzymatic activity of X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1:
3.3.2.10;

Protein crystallography data

The structure of X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1, PDB code: 1ehy was solved by M.Nardini, I.S.Ridder, H.J.Rozeboom, K.H.Kalk, R.Rink, D.B.Janssen, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.10
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 146.624, 100.201, 96.879, 90.00, 100.68, 90.00
R / Rfree (%) 19 / 22.7

Potassium Binding Sites:

The binding sites of Potassium atom in the X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1 (pdb code 1ehy). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1, PDB code: 1ehy:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 1ehy

Go back to Potassium Binding Sites List in 1ehy
Potassium binding site 1 out of 4 in the X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K295

b:36.6
occ:1.00
O A:SER184 2.4 22.9 1.0
O A:HOH411 2.6 31.2 1.0
O A:ARG186 2.6 36.4 1.0
O A:ASP181 2.8 30.1 1.0
O A:HOH352 2.9 41.6 1.0
C A:SER184 3.5 30.0 1.0
O A:TYR185 3.5 37.2 1.0
C A:ARG186 3.6 33.6 1.0
C A:ASP181 3.8 27.4 1.0
C A:TYR185 3.9 35.7 1.0
CA A:ASP187 4.1 33.1 1.0
N A:SER184 4.2 28.5 1.0
N A:ASP187 4.2 33.1 1.0
CA A:SER184 4.2 29.2 1.0
O A:HIS182 4.3 25.4 1.0
CB A:SER184 4.4 25.2 1.0
CA A:HIS182 4.4 25.5 1.0
N A:ARG186 4.4 35.3 1.0
O A:HOH392 4.4 49.0 1.0
N A:TYR185 4.4 30.9 1.0
O A:ASP187 4.4 34.3 1.0
C A:HIS182 4.4 24.5 1.0
C A:ASP187 4.5 33.8 1.0
N A:HIS182 4.5 26.5 1.0
CA A:TYR185 4.5 34.1 1.0
CA A:ARG186 4.6 34.4 1.0
CB A:ASP246 4.7 71.9 1.0
CA A:ASP181 4.8 28.3 1.0
OD1 A:ASP187 4.8 38.1 1.0

Potassium binding site 2 out of 4 in 1ehy

Go back to Potassium Binding Sites List in 1ehy
Potassium binding site 2 out of 4 in the X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K296

b:29.9
occ:1.00
O B:ASP181 2.6 27.5 1.0
O B:ARG186 2.7 31.8 1.0
O B:SER184 2.7 25.4 1.0
O B:HOH359 2.9 54.7 1.0
O B:HOH440 3.0 31.1 1.0
C B:SER184 3.6 23.4 1.0
C B:ARG186 3.6 31.6 1.0
C B:ASP181 3.7 26.7 1.0
O B:TYR185 3.8 33.8 1.0
C B:TYR185 4.0 30.7 1.0
O B:ASP187 4.2 33.8 1.0
CA B:ASP187 4.3 33.2 1.0
N B:ARG186 4.3 31.4 1.0
O B:HIS182 4.3 25.5 1.0
N B:ASP187 4.4 30.9 1.0
O B:HOH401 4.4 47.0 1.0
N B:SER184 4.4 20.7 1.0
CA B:SER184 4.4 21.2 1.0
CA B:HIS182 4.4 26.6 1.0
N B:TYR185 4.4 25.3 1.0
N B:HIS182 4.4 25.4 1.0
C B:HIS182 4.5 24.1 1.0
CA B:TYR185 4.5 28.7 1.0
C B:ASP187 4.5 33.7 1.0
CB B:SER184 4.5 21.2 1.0
CA B:ARG186 4.6 31.1 1.0
CA B:ASP181 4.6 25.0 1.0
CB B:ASP181 5.0 27.9 1.0

Potassium binding site 3 out of 4 in 1ehy

Go back to Potassium Binding Sites List in 1ehy
Potassium binding site 3 out of 4 in the X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K297

b:33.3
occ:1.00
O C:ARG186 2.6 32.7 1.0
O C:ASP181 2.6 26.6 1.0
O C:HOH559 2.8 36.0 1.0
O C:SER184 2.9 26.7 1.0
O C:TYR185 3.6 27.8 1.0
C C:ARG186 3.6 31.9 1.0
C C:ASP181 3.6 26.5 1.0
C C:SER184 3.7 26.1 1.0
C C:TYR185 4.0 29.2 1.0
O C:ASP187 4.2 35.5 1.0
CA C:ASP187 4.2 35.4 1.0
CA C:HIS182 4.3 26.2 1.0
N C:ASP187 4.3 33.9 1.0
N C:SER184 4.3 21.6 1.0
O C:HIS182 4.4 29.6 1.0
N C:HIS182 4.4 24.5 1.0
C C:HIS182 4.4 25.9 1.0
CA C:SER184 4.4 23.8 1.0
O C:HOH601 4.4 44.9 1.0
C C:ASP187 4.4 34.0 1.0
N C:ARG186 4.5 28.7 1.0
N C:TYR185 4.5 27.6 1.0
CB C:SER184 4.6 21.2 1.0
CA C:ASP181 4.6 28.1 1.0
CA C:TYR185 4.6 29.0 1.0
CA C:ARG186 4.6 28.7 1.0

Potassium binding site 4 out of 4 in 1ehy

Go back to Potassium Binding Sites List in 1ehy
Potassium binding site 4 out of 4 in the X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of X-Ray Structure of the Epoxide Hydrolase From Agrobacterium Radiobacter AD1 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K298

b:33.5
occ:1.00
O D:SER184 2.6 28.4 1.0
O D:ASP181 2.6 24.5 1.0
O D:ARG186 2.7 28.2 1.0
O D:TYR185 3.4 29.4 1.0
C D:SER184 3.5 24.9 1.0
C D:ASP181 3.7 23.0 1.0
C D:ARG186 3.7 28.2 1.0
C D:TYR185 3.9 29.1 1.0
O D:ASP187 4.2 29.4 1.0
CA D:ASP187 4.2 30.8 1.0
N D:SER184 4.3 21.1 1.0
CA D:SER184 4.3 22.6 1.0
N D:TYR185 4.3 25.3 1.0
N D:ASP187 4.4 28.9 1.0
CA D:HIS182 4.4 25.8 1.0
O D:HIS182 4.4 25.9 1.0
O D:HOH382 4.4 67.0 1.0
N D:HIS182 4.4 24.1 1.0
C D:HIS182 4.4 26.0 1.0
CA D:TYR185 4.5 30.9 1.0
C D:ASP187 4.5 30.1 1.0
N D:ARG186 4.5 27.9 1.0
CB D:SER184 4.5 21.2 1.0
CA D:ASP181 4.7 24.0 1.0
CA D:ARG186 4.7 27.3 1.0

Reference:

M.Nardini, I.S.Ridder, H.J.Rozeboom, K.H.Kalk, R.Rink, D.B.Janssen, B.W.Dijkstra. The X-Ray Structure of Epoxide Hydrolase From Agrobacterium Radiobacter AD1. An Enzyme to Detoxify Harmful Epoxides. J.Biol.Chem. V. 274 14579 1999.
ISSN: ISSN 0021-9258
PubMed: 10329649
DOI: 10.1074/JBC.274.21.14579
Page generated: Mon Aug 12 04:26:25 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy