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Sodium in PDB 2j5n: 1-Pyrroline-5-Carboxylate Dehydrogenase From Thermus Thermophirus with Bound Inhibitor Glycine and Nad.

Enzymatic activity of 1-Pyrroline-5-Carboxylate Dehydrogenase From Thermus Thermophirus with Bound Inhibitor Glycine and Nad.

All present enzymatic activity of 1-Pyrroline-5-Carboxylate Dehydrogenase From Thermus Thermophirus with Bound Inhibitor Glycine and Nad.:
1.5.1.12;

Protein crystallography data

The structure of 1-Pyrroline-5-Carboxylate Dehydrogenase From Thermus Thermophirus with Bound Inhibitor Glycine and Nad., PDB code: 2j5n was solved by E.Inagaki, K.Sakamoto, M.Nishio, S.Yokoyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 92.85 / 1.63
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 102.589, 102.589, 278.637, 90.00, 90.00, 120.00
R / Rfree (%) 14.6 / 17.4

Sodium Binding Sites:

The binding sites of Sodium atom in the 1-Pyrroline-5-Carboxylate Dehydrogenase From Thermus Thermophirus with Bound Inhibitor Glycine and Nad. (pdb code 2j5n). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the 1-Pyrroline-5-Carboxylate Dehydrogenase From Thermus Thermophirus with Bound Inhibitor Glycine and Nad., PDB code: 2j5n:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 2j5n

Go back to Sodium Binding Sites List in 2j5n
Sodium binding site 1 out of 2 in the 1-Pyrroline-5-Carboxylate Dehydrogenase From Thermus Thermophirus with Bound Inhibitor Glycine and Nad.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of 1-Pyrroline-5-Carboxylate Dehydrogenase From Thermus Thermophirus with Bound Inhibitor Glycine and Nad. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1525

b:18.3
occ:1.00
O A:HOH2426 2.5 28.2 1.0
O A:HOH2143 2.5 25.7 1.0
O A:LEU56 2.6 11.9 1.0
O A:GLU123 2.7 7.7 1.0
O A:ASP211 2.8 11.7 1.0
OG A:SER55 3.0 12.1 1.0
CG A:GLU123 3.5 8.6 1.0
N A:LEU56 3.6 11.3 1.0
C A:LEU56 3.7 11.1 1.0
C A:GLU123 3.8 8.1 1.0
C A:ASP211 3.8 10.8 1.0
C A:SER55 4.1 11.8 1.0
CB A:SER55 4.2 12.2 1.0
CA A:LEU56 4.2 11.3 1.0
CA A:ASP211 4.2 11.3 1.0
CA A:GLU123 4.3 7.6 1.0
CA A:SER55 4.3 11.8 1.0
O A:HOH2425 4.3 21.5 1.0
OE1 A:GLU123 4.5 8.6 1.0
CD A:PRO58 4.5 10.0 1.0
CB A:ASP211 4.5 11.9 1.0
CD A:GLU123 4.5 9.0 1.0
CB A:GLU123 4.5 7.5 1.0
OD1 A:ASP211 4.7 18.2 1.0
N A:ASN57 4.8 10.7 1.0
N A:VAL124 4.9 7.7 1.0
CB A:LEU56 4.9 11.5 1.0
N A:ALA212 5.0 9.9 1.0
O A:SER55 5.0 12.6 1.0

Sodium binding site 2 out of 2 in 2j5n

Go back to Sodium Binding Sites List in 2j5n
Sodium binding site 2 out of 2 in the 1-Pyrroline-5-Carboxylate Dehydrogenase From Thermus Thermophirus with Bound Inhibitor Glycine and Nad.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of 1-Pyrroline-5-Carboxylate Dehydrogenase From Thermus Thermophirus with Bound Inhibitor Glycine and Nad. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na1526

b:18.5
occ:1.00
O B:HOH2420 2.4 28.0 1.0
O B:GLU123 2.5 9.3 1.0
O B:LEU56 2.5 10.9 1.0
O B:HOH2132 2.8 24.7 1.0
O B:ASP211 3.0 11.5 1.0
OG B:SER55 3.2 11.9 1.0
CG B:GLU123 3.6 10.3 1.0
C B:GLU123 3.6 8.9 1.0
C B:LEU56 3.6 11.7 1.0
N B:LEU56 3.7 11.6 1.0
C B:ASP211 4.0 10.8 1.0
CA B:GLU123 4.1 8.9 1.0
CA B:LEU56 4.2 11.7 1.0
CD B:PRO58 4.3 10.4 1.0
O B:HOH2421 4.3 30.4 1.0
CA B:ASP211 4.4 11.3 1.0
C B:SER55 4.4 11.9 1.0
CB B:SER55 4.5 12.6 1.0
CB B:GLU123 4.5 9.4 1.0
CA B:SER55 4.6 11.8 1.0
CB B:ASP211 4.6 12.2 1.0
CD B:GLU123 4.6 10.7 1.0
OE1 B:GLU123 4.6 10.6 1.0
OD1 B:ASP211 4.7 19.8 1.0
N B:VAL124 4.7 8.2 1.0
N B:ASN57 4.8 10.4 1.0
O B:VAL364 4.8 10.2 1.0
CB B:LEU56 4.9 12.3 1.0
CG1 B:VAL124 5.0 8.2 1.0
CG2 B:VAL65 5.0 15.2 1.0

Reference:

E.Inagaki, K.Sakamoto, M.Nishio, S.Yokoyama, T.H.Tahirov. Crystal Structure of Ternary Complex of DELTA1-Pyrroline-5-Carboxylate Dehydrogenase with Substrate Mimic and Co-Factoer To Be Published.
Page generated: Mon Oct 7 02:57:06 2024

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