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Potassium in PDB 1arz: Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate

Enzymatic activity of Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate

All present enzymatic activity of Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate:
1.3.1.26;

Protein crystallography data

The structure of Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate, PDB code: 1arz was solved by G.Scapin, S.G.Reddy, R.Zheng, J.S.Blanchard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 137.600, 123.800, 66.600, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 29.7

Potassium Binding Sites:

The binding sites of Potassium atom in the Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate (pdb code 1arz). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate, PDB code: 1arz:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1arz

Go back to Potassium Binding Sites List in 1arz
Potassium binding site 1 out of 2 in the Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K301

b:29.5
occ:1.00
O B:LEU28 2.2 33.4 1.0
O B:HOH411 2.3 5.3 1.0
O B:ALA25 2.5 27.0 1.0
O B:VAL31 2.5 18.0 1.0
O B:LEU26 2.8 25.4 1.0
C B:LEU28 3.2 33.7 1.0
O B:HOH439 3.3 30.8 1.0
C B:LEU26 3.4 22.8 1.0
C B:ALA25 3.6 23.7 1.0
N B:LEU28 3.6 32.1 1.0
C B:VAL31 3.7 24.9 1.0
CA B:LEU26 3.8 19.9 1.0
CA B:LEU28 3.8 33.4 1.0
N B:LEU26 4.2 19.2 1.0
CG2 B:VAL31 4.2 18.3 1.0
N B:GLU29 4.2 26.4 1.0
N B:ALA27 4.4 27.7 1.0
C B:ALA27 4.4 30.9 1.0
CA B:GLN32 4.4 29.3 1.0
N B:VAL31 4.5 25.8 1.0
N B:GLN32 4.5 28.7 1.0
CA B:GLU29 4.5 24.9 1.0
CB B:LEU28 4.6 39.0 1.0
CA B:VAL31 4.7 24.1 1.0
OE1 B:GLU29 4.8 25.9 1.0
CA B:ALA25 4.9 26.6 1.0
O B:HOH404 4.9 12.7 1.0
C B:GLU29 4.9 23.8 1.0
CA B:ALA27 4.9 30.2 1.0
N B:GLY30 5.0 19.0 1.0

Potassium binding site 2 out of 2 in 1arz

Go back to Potassium Binding Sites List in 1arz
Potassium binding site 2 out of 2 in the Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K301

b:24.9
occ:1.00
O D:LEU26 2.5 32.8 1.0
O D:VAL31 2.6 19.5 1.0
O D:LEU28 2.7 28.4 1.0
O D:ALA25 2.9 31.1 1.0
N D:ASP3 3.3 63.1 1.0
C D:LEU26 3.4 24.3 1.0
C D:LEU28 3.5 23.8 1.0
C D:VAL31 3.8 20.7 1.0
N D:LEU28 3.9 23.3 1.0
CA D:LEU26 4.0 20.6 1.0
C D:ALA25 4.0 28.2 1.0
CA D:LEU28 4.2 22.7 1.0
CA D:ASP3 4.2 61.1 1.0
C D:ALA27 4.3 24.4 1.0
N D:GLU29 4.3 20.3 1.0
N D:VAL31 4.3 15.1 1.0
N D:ALA27 4.4 24.6 1.0
CG1 D:VAL31 4.4 22.6 1.0
CA D:VAL31 4.5 21.5 1.0
N D:LEU26 4.5 25.1 1.0
CA D:GLU29 4.5 18.0 1.0
CA D:ALA27 4.7 25.9 1.0
O D:ALA27 4.7 29.3 1.0
OE2 D:GLU29 4.8 35.4 1.0
CB D:ASP3 4.8 58.2 1.0
N D:GLN32 4.8 17.4 1.0
CA D:GLN32 4.9 25.9 1.0
C D:GLU29 5.0 19.9 1.0
CB D:VAL31 5.0 26.5 1.0

Reference:

G.Scapin, S.G.Reddy, R.Zheng, J.S.Blanchard. Three-Dimensional Structure of Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and the Inhibitor 2,6-Pyridinedicarboxylate. Biochemistry V. 36 15081 1997.
ISSN: ISSN 0006-2960
PubMed: 9398235
DOI: 10.1021/BI9719915
Page generated: Sun Dec 13 22:41:39 2020

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