Potassium in PDB 6uk3: Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine

Enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine

All present enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine:
3.3.1.1;

Protein crystallography data

The structure of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine, PDB code: 6uk3 was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 96.030, 112.730, 105.920, 90.00, 114.73, 90.00
R / Rfree (%) 13 / 16.1

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine (pdb code 6uk3). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine, PDB code: 6uk3:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 6uk3

Go back to Potassium Binding Sites List in 6uk3
Potassium binding site 1 out of 4 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K504

b:13.3
occ:0.72
 O A:THR398 2.7 13.1 1.0
O A:HIS400 2.8 12.3 1.0
O A:HOH934 2.9 15.1 1.0
OG1 A:THR398 2.9 14.6 1.0
O A:HOH879 2.9 13.7 1.0
O D:HOH702 2.9 13.4 1.0
OE1 A:GLN68 3.1 13.4 1.0
CD A:GLN68 3.5 12.4 1.0
NE2 A:GLN68 3.5 13.1 1.0
CB A:THR398 3.5 13.6 1.0
C A:THR398 3.6 12.1 1.0
O A:GLY399 3.6 11.2 1.0
C A:HIS400 3.7 11.9 1.0
N6 A:ADN502 3.9 12.7 1.0
C A:GLY399 4.0 11.4 1.0
CA A:PRO401 4.1 11.3 1.0
CA A:THR398 4.2 12.9 1.0
N A:PRO401 4.2 11.7 1.0
CB D:ASP254 4.3 13.3 1.0
N A:GLY399 4.5 12.5 1.0
O A:HOH1000 4.5 14.1 1.0
N A:HIS400 4.5 11.9 1.0
CG D:ASP254 4.6 14.1 1.0
NE2 A:GLN94 4.6 18.5 1.0
CG A:GLN68 4.6 12.1 1.0
CA A:GLY399 4.6 12.4 1.0
OD1 D:ASP254 4.7 14.8 1.0
CA A:HIS400 4.7 11.5 1.0
C A:PRO401 4.7 11.2 1.0
N A:SER402 4.8 11.2 1.0
CG2 A:THR398 4.8 15.8 1.0
O D:HOH710 4.9 16.4 1.0
O D:ASP254 4.9 13.9 1.0

Potassium binding site 2 out of 4 in 6uk3

Go back to Potassium Binding Sites List in 6uk3
Potassium binding site 2 out of 4 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K507

b:13.2
occ:0.76
 O B:THR398 2.8 12.6 1.0
O B:HIS400 2.8 11.7 1.0
O B:HOH897 2.9 14.4 1.0
O B:HOH844 2.9 15.0 1.0
OG1 B:THR398 2.9 13.8 1.0
O C:HOH728 2.9 13.1 1.0
OE1 B:GLN68 3.1 13.5 1.0
NE2 B:GLN68 3.4 13.5 1.0
CD B:GLN68 3.4 12.7 1.0
CB B:THR398 3.5 12.9 1.0
C B:THR398 3.6 11.1 1.0
O B:GLY399 3.6 11.7 1.0
C B:HIS400 3.7 11.1 1.0
N6 B:ADN502 3.9 12.3 1.0
C B:GLY399 4.0 11.9 1.0
CA B:PRO401 4.1 11.4 1.0
CA B:THR398 4.2 11.6 1.0
N B:PRO401 4.2 11.6 1.0
CB C:ASP254 4.3 12.6 1.0
N B:GLY399 4.5 11.2 1.0
O B:HOH957 4.5 14.2 1.0
N B:HIS400 4.5 11.5 1.0
CG C:ASP254 4.6 12.9 1.0
NE2 B:GLN94 4.6 16.7 1.0
CG B:GLN68 4.6 12.8 1.0
CA B:GLY399 4.6 12.0 1.0
OD1 C:ASP254 4.7 13.8 1.0
CA B:HIS400 4.7 11.4 1.0
C B:PRO401 4.7 11.3 1.0
N B:SER402 4.8 11.1 1.0
CG2 B:THR398 4.9 13.9 1.0
O C:HOH737 4.9 16.8 1.0
O C:ASP254 5.0 12.7 1.0

Potassium binding site 3 out of 4 in 6uk3

Go back to Potassium Binding Sites List in 6uk3
Potassium binding site 3 out of 4 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K506

b:13.8
occ:0.77
 O C:THR398 2.8 12.3 1.0
O C:HIS400 2.8 12.8 1.0
O C:HOH853 2.9 13.5 1.0
O B:HOH710 2.9 13.3 1.0
OG1 C:THR398 2.9 13.0 1.0
O C:HOH906 2.9 15.3 1.0
OE1 C:GLN68 3.2 13.6 1.0
NE2 C:GLN68 3.4 13.5 1.0
CD C:GLN68 3.5 12.8 1.0
CB C:THR398 3.5 13.1 1.0
O C:GLY399 3.6 12.2 1.0
C C:THR398 3.6 11.2 1.0
C C:HIS400 3.7 12.3 1.0
N6 C:ADN502 4.0 12.9 1.0
C C:GLY399 4.0 11.4 1.0
CA C:PRO401 4.0 12.5 1.0
N C:PRO401 4.2 12.7 1.0
CA C:THR398 4.2 12.0 1.0
CB B:ASP254 4.3 12.5 1.0
O C:HOH974 4.4 13.7 1.0
N C:GLY399 4.5 11.1 1.0
N C:HIS400 4.5 11.9 1.0
CG B:ASP254 4.5 13.0 1.0
NE2 C:GLN94 4.6 17.0 1.0
CG C:GLN68 4.6 13.5 1.0
OD1 B:ASP254 4.6 13.0 1.0
CA C:GLY399 4.6 11.9 1.0
C C:PRO401 4.7 12.6 1.0
CA C:HIS400 4.7 11.8 1.0
N C:SER402 4.8 11.6 1.0
CG2 C:THR398 4.9 14.5 1.0
O B:HOH718 4.9 16.2 1.0
O B:ASP254 4.9 13.0 1.0

Potassium binding site 4 out of 4 in 6uk3

Go back to Potassium Binding Sites List in 6uk3
Potassium binding site 4 out of 4 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K508

b:15.5
occ:0.78
 O D:THR398 2.8 15.0 1.0
O D:HIS400 2.8 14.4 1.0
O D:HOH915 2.9 16.0 1.0
O D:HOH857 2.9 16.6 1.0
OG1 D:THR398 2.9 15.3 1.0
O A:HOH698 2.9 15.1 1.0
OE1 D:GLN68 3.2 14.8 1.0
NE2 D:GLN68 3.4 14.9 1.0
CD D:GLN68 3.5 14.5 1.0
CB D:THR398 3.5 14.4 1.0
O D:GLY399 3.6 13.2 1.0
C D:THR398 3.6 13.3 1.0
C D:HIS400 3.7 13.9 1.0
N6 D:ADN502 4.0 14.0 1.0
C D:GLY399 4.0 12.9 1.0
CA D:PRO401 4.0 13.1 1.0
CA D:THR398 4.2 13.6 1.0
N D:PRO401 4.2 14.0 1.0
CB A:ASP254 4.3 14.6 1.0
O D:HOH959 4.4 16.4 1.0
N D:GLY399 4.5 13.0 1.0
N D:HIS400 4.5 13.5 1.0
CG A:ASP254 4.5 14.4 1.0
NE2 D:GLN94 4.6 19.9 1.0
CG D:GLN68 4.6 14.5 1.0
CA D:GLY399 4.6 13.6 1.0
OD1 A:ASP254 4.7 15.6 1.0
CA D:HIS400 4.7 13.2 1.0
C D:PRO401 4.7 12.9 1.0
N D:SER402 4.8 13.2 1.0
CG2 D:THR398 4.8 16.1 1.0
O A:HOH713 4.9 18.4 1.0
O A:ASP254 5.0 14.7 1.0

Reference:

C.T.Romanaggi, D.M.Dranow, J.Abendroth, D.D.Lorimer, P.S.Horanyi, T.E.Edwards. Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Acanthamoeba Castellanii with Bound Nad and Adenosine To Be Published.
Page generated: Mon Dec 14 01:49:29 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy