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Potassium in PDB 1dhp: Dihydrodipicolinate Synthase

Enzymatic activity of Dihydrodipicolinate Synthase

All present enzymatic activity of Dihydrodipicolinate Synthase:
4.2.1.52;

Protein crystallography data

The structure of Dihydrodipicolinate Synthase, PDB code: 1dhp was solved by C.Mirwaldt, I.Korndoerfer, R.Huber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.30
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 122.410, 122.410, 111.220, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / n/a

Potassium Binding Sites:

The binding sites of Potassium atom in the Dihydrodipicolinate Synthase (pdb code 1dhp). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Dihydrodipicolinate Synthase, PDB code: 1dhp:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1dhp

Go back to Potassium Binding Sites List in 1dhp
Potassium binding site 1 out of 2 in the Dihydrodipicolinate Synthase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Dihydrodipicolinate Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K293

b:34.0
occ:1.00
O A:VAL154 2.6 28.0 1.0
O A:ILE157 2.7 24.6 1.0
O A:ALA152 3.0 28.1 1.0
O A:LYS155 3.3 38.3 1.0
C A:VAL154 3.6 31.3 1.0
C A:LYS155 3.6 38.0 1.0
C A:ILE157 3.7 23.1 1.0
CA A:LYS155 3.7 38.8 1.0
C A:ALA152 3.9 26.1 1.0
N A:LYS155 4.0 34.9 1.0
N A:ILE157 4.2 26.5 1.0
CA A:ILE157 4.5 23.4 1.0
N A:VAL154 4.5 30.2 1.0
CA A:ALA152 4.5 23.7 1.0
N A:ASN156 4.5 36.1 1.0
C A:LYS153 4.6 30.8 1.0
N A:ILE158 4.6 22.9 1.0
CA A:ILE158 4.7 22.7 1.0
CA A:VAL154 4.7 29.5 1.0
N A:LYS153 4.8 27.4 1.0
CB A:ILE157 4.9 22.2 1.0
C A:ASN156 4.9 30.4 1.0
O A:LYS153 4.9 32.5 1.0
CA A:LYS153 4.9 30.2 1.0

Potassium binding site 2 out of 2 in 1dhp

Go back to Potassium Binding Sites List in 1dhp
Potassium binding site 2 out of 2 in the Dihydrodipicolinate Synthase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Dihydrodipicolinate Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K293

b:27.8
occ:1.00
O B:ILE157 2.6 21.3 1.0
O B:ALA152 2.7 25.1 1.0
O B:HOH400 2.7 47.3 1.0
O B:VAL154 2.9 29.4 1.0
O B:HOH365 3.4 55.7 1.0
O B:LYS155 3.4 30.4 1.0
C B:ILE157 3.7 18.6 1.0
C B:LYS155 3.8 32.0 1.0
C B:VAL154 3.8 28.8 1.0
C B:ALA152 3.8 23.6 1.0
CA B:LYS155 4.0 34.3 1.0
N B:LYS155 4.3 32.4 1.0
N B:ILE157 4.3 21.4 1.0
CA B:ALA152 4.4 23.1 1.0
CA B:ILE157 4.6 18.4 1.0
N B:ILE158 4.6 18.6 1.0
N B:VAL154 4.6 27.3 1.0
C B:LYS153 4.6 27.4 1.0
N B:ASN156 4.6 29.8 1.0
CA B:ILE158 4.6 17.7 1.0
N B:LYS153 4.8 24.9 1.0
O B:LYS153 4.8 28.2 1.0
CA B:VAL154 4.9 25.6 1.0
C B:ASN156 5.0 23.8 1.0
CA B:LYS153 5.0 26.1 1.0
CB B:ILE157 5.0 16.0 1.0
CD1 B:PHE181 5.0 16.9 1.0

Reference:

C.Mirwaldt, I.Korndorfer, R.Huber. The Crystal Structure of Dihydrodipicolinate Synthase From Escherichia Coli at 2.5 A Resolution. J.Mol.Biol. V. 246 227 1995.
ISSN: ISSN 0022-2836
PubMed: 7853400
DOI: 10.1006/JMBI.1994.0078
Page generated: Sat Aug 9 01:49:38 2025

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