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Potassium in PDB 2a6n: Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A

Enzymatic activity of Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A

All present enzymatic activity of Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A:
4.2.1.52;

Protein crystallography data

The structure of Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A, PDB code: 2a6n was solved by R.C.Dobson, S.R.Devenish, L.A.Turner, V.R.Clifford, F.G.Pearce, G.B.Jameson, J.A.Gerrard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.33 / 1.94
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 120.989, 120.989, 111.302, 90.00, 90.00, 120.00
R / Rfree (%) 16.3 / 19.1

Potassium Binding Sites:

The binding sites of Potassium atom in the Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A (pdb code 2a6n). 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 (E. Coli)- Mutant R138A, PDB code: 2a6n:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 2a6n

Go back to Potassium Binding Sites List in 2a6n
Potassium binding site 1 out of 2 in the Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K600

b:28.5
occ:1.00
O A:VAL154 2.6 29.3 1.0
O A:ILE157 2.6 23.8 1.0
O A:ALA152 2.7 25.0 1.0
O A:HOH787 2.8 39.0 1.0
O A:LYS155 3.1 29.1 1.0
C A:ILE157 3.7 24.2 1.0
C A:VAL154 3.7 29.3 1.0
C A:LYS155 3.7 29.3 1.0
C A:ALA152 3.8 25.2 1.0
CA A:LYS155 4.0 30.1 1.0
N A:ILE157 4.2 25.6 1.0
N A:LYS155 4.3 30.0 1.0
CA A:ALA152 4.4 24.1 1.0
CA A:ILE157 4.5 24.6 1.0
O A:HOH831 4.5 42.3 1.0
O A:HOH847 4.5 44.7 1.0
N A:VAL154 4.5 28.6 1.0
CG2 A:ILE158 4.5 26.9 1.0
N A:ILE158 4.6 23.6 1.0
CA A:ILE158 4.6 24.0 1.0
C A:LYS153 4.6 28.2 1.0
N A:ASN156 4.6 28.3 1.0
N A:LYS153 4.8 25.6 1.0
CA A:VAL154 4.8 29.1 1.0
CB A:ILE157 4.9 24.5 1.0
O A:LYS153 4.9 28.5 1.0
CD1 A:PHE181 4.9 25.1 1.0
CA A:LYS153 4.9 27.5 1.0

Potassium binding site 2 out of 2 in 2a6n

Go back to Potassium Binding Sites List in 2a6n
Potassium binding site 2 out of 2 in the Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K601

b:24.8
occ:1.00
O B:ILE157 2.6 20.4 1.0
O B:VAL154 2.7 25.9 1.0
O B:ALA152 2.7 21.3 1.0
O B:HOH744 2.7 31.8 1.0
O B:HOH914 3.0 47.7 1.0
O B:LYS155 3.2 23.9 1.0
C B:VAL154 3.7 26.0 1.0
C B:ILE157 3.7 20.0 1.0
C B:LYS155 3.7 25.0 1.0
C B:ALA152 3.7 21.6 1.0
CA B:LYS155 4.1 26.0 1.0
N B:ILE157 4.2 20.5 1.0
O B:HOH867 4.2 42.1 1.0
N B:LYS155 4.3 25.9 1.0
CA B:ALA152 4.4 20.5 1.0
CA B:ILE157 4.5 20.1 1.0
N B:VAL154 4.5 25.4 1.0
C B:LYS153 4.6 25.4 1.0
N B:ASN156 4.6 23.2 1.0
N B:ILE158 4.6 19.3 1.0
CA B:ILE158 4.7 19.8 1.0
N B:LYS153 4.7 22.8 1.0
CA B:VAL154 4.8 25.7 1.0
CD1 B:PHE181 4.8 18.8 1.0
O B:LYS153 4.9 25.8 1.0
CA B:LYS153 4.9 24.5 1.0
CB B:ILE157 4.9 19.6 1.0
C B:ASN156 5.0 20.9 1.0

Reference:

R.C.Dobson, S.R.Devenish, L.A.Turner, V.R.Clifford, F.G.Pearce, G.B.Jameson, J.A.Gerrard. Role of Arginine 138 in the Catalysis and Regulation of Escherichia Coli Dihydrodipicolinate Synthase. Biochemistry V. 44 13007 2005.
ISSN: ISSN 0006-2960
PubMed: 16185069
DOI: 10.1021/BI051281W
Page generated: Mon Aug 12 05:59:26 2024

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