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Potassium in PDB 3n58: Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form

Enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form

All present enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form:
3.3.1.1;

Protein crystallography data

The structure of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form, PDB code: 3n58 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) 49.27 / 2.39
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.450, 165.230, 184.140, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 23.5

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form (pdb code 3n58). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form, PDB code: 3n58:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in 3n58

Go back to Potassium Binding Sites List in 3n58
Potassium binding site 1 out of 3 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form


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 Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K2

b:33.1
occ:1.00
O A:THR385 3.0 14.1 1.0
O A:HIS387 3.0 17.4 1.0
O A:HOH521 3.1 11.9 1.0
OG1 A:THR385 3.2 12.4 1.0
O A:HOH517 3.3 29.3 1.0
O A:HOH547 3.4 35.7 1.0
OE1 A:GLN59 3.5 24.3 1.0
NE2 A:GLN59 3.5 14.2 1.0
O A:GLY386 3.6 16.1 1.0
CD A:GLN59 3.7 24.9 1.0
C A:HIS387 3.7 31.1 1.0
C A:THR385 3.7 19.1 1.0
CB A:THR385 3.8 17.9 1.0
N6 A:ADN500 3.9 7.1 1.0
C A:GLY386 4.0 21.2 1.0
CA A:PRO388 4.0 15.6 1.0
N A:PRO388 4.1 19.6 1.0
CB C:ASP244 4.3 20.7 1.0
CA A:THR385 4.4 12.1 1.0
N A:HIS387 4.4 13.7 1.0
N A:GLY386 4.5 15.1 1.0
C A:PRO388 4.6 18.4 1.0
CG C:ASP244 4.6 30.5 1.0
CA A:GLY386 4.6 12.4 1.0
N A:SER389 4.7 15.6 1.0
CA A:HIS387 4.7 22.7 1.0
OD1 C:ASP244 4.7 21.1 1.0
CG A:GLN59 4.8 20.4 1.0
O C:ASP244 4.8 29.4 1.0
OE1 A:GLN85 4.8 19.9 1.0

Potassium binding site 2 out of 3 in 3n58

Go back to Potassium Binding Sites List in 3n58
Potassium binding site 2 out of 3 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form


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 Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1

b:33.0
occ:1.00
O C:THR385 2.9 13.4 1.0
O C:HOH479 3.0 15.9 1.0
O C:HIS387 3.0 20.8 1.0
O C:HOH520 3.2 19.4 1.0
OG1 C:THR385 3.2 19.8 1.0
OE1 C:GLN59 3.3 20.8 1.0
O A:HOH498 3.5 33.6 1.0
NE2 C:GLN59 3.5 20.5 1.0
CD C:GLN59 3.6 22.0 1.0
CB C:THR385 3.7 22.2 1.0
O C:GLY386 3.7 23.2 1.0
C C:HIS387 3.7 26.4 1.0
C C:THR385 3.7 21.3 1.0
N6 C:ADN500 4.0 22.0 1.0
C C:GLY386 4.0 21.3 1.0
CA C:PRO388 4.1 20.9 1.0
N C:PRO388 4.2 28.2 1.0
CB A:ASP244 4.3 25.7 1.0
CA C:THR385 4.4 6.7 1.0
N C:HIS387 4.4 9.8 1.0
O C:HOH589 4.5 20.8 1.0
CG A:ASP244 4.6 30.4 1.0
N C:GLY386 4.6 14.3 1.0
OD1 A:ASP244 4.6 26.6 1.0
CA C:HIS387 4.6 27.3 1.0
CA C:GLY386 4.6 14.0 1.0
C C:PRO388 4.7 20.8 1.0
OE1 C:GLN85 4.7 15.9 1.0
CG C:GLN59 4.7 21.4 1.0
N C:SER389 4.8 22.6 1.0
O A:ASP244 4.9 27.1 1.0
O A:HOH626 5.0 21.7 1.0
CG2 C:THR385 5.0 9.0 1.0

Potassium binding site 3 out of 3 in 3n58

Go back to Potassium Binding Sites List in 3n58
Potassium binding site 3 out of 3 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form


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 Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K467

b:43.1
occ:1.00
O D:HIS387 3.0 22.4 1.0
O D:THR385 3.0 22.9 1.0
O D:HOH539 3.1 37.2 1.0
OG1 D:THR385 3.2 16.3 1.0
OE1 D:GLN59 3.3 24.9 1.0
NE2 D:GLN59 3.5 24.6 1.0
O B:HOH635 3.6 27.6 1.0
CD D:GLN59 3.6 32.1 1.0
O D:GLY386 3.7 27.0 1.0
C D:HIS387 3.7 21.6 1.0
CB D:THR385 3.8 23.8 1.0
C D:THR385 3.9 24.5 1.0
CA D:PRO388 4.0 18.4 1.0
C D:GLY386 4.2 23.2 1.0
N D:PRO388 4.2 25.2 1.0
CB B:ASP244 4.2 30.1 1.0
N6 D:ADN500 4.2 32.0 1.0
OD1 B:ASP244 4.4 36.5 1.0
N D:HIS387 4.5 16.1 1.0
CA D:THR385 4.5 19.9 1.0
CG B:ASP244 4.6 36.5 1.0
O B:ASP244 4.6 32.7 1.0
C D:PRO388 4.6 30.6 1.0
CG D:GLN59 4.7 31.6 1.0
CA D:HIS387 4.7 26.9 1.0
N D:SER389 4.8 23.1 1.0
OE1 D:GLN85 4.8 34.4 1.0
N D:GLY386 4.8 20.5 1.0
CA D:GLY386 5.0 15.8 1.0
O D:HOH622 5.0 33.5 1.0

Reference:

Ssgcid, A.Gardberg, B.Sankaran, J.Abendroth, B.Staker. Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From Brucella Melitensis in Ternary Complex with Nad and Adenosine, Orthorhombic Form To Be Published.
Page generated: Mon Aug 12 08:49:07 2024

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