Potassium in PDB 3i7q: Dihydrodipicolinate Synthase Mutant - K161A

All present enzymatic activity of Dihydrodipicolinate Synthase Mutant - K161A:
4.2.1.52;

The structure of Dihydrodipicolinate Synthase Mutant - K161A, PDB code: 3i7q was solved by R.C.J.Dobson, G.B.Jameson, J.A.Gerrard, T.P.Soares Da Costa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.84 / 2.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.044, 121.044, 110.501, 90.00, 90.00, 120.00
R / Rfree (%)	20.4 / 23.7

The binding sites of Potassium atom in the Dihydrodipicolinate Synthase Mutant - K161A (pdb code 3i7q). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Dihydrodipicolinate Synthase Mutant - K161A, PDB code: 3i7q:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in the Dihydrodipicolinate Synthase Mutant - K161A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Dihydrodipicolinate Synthase Mutant - K161A within 5.0Å range: probe atom residue distance (Å) B Occ A:K295 b:36.1 occ:1.00 O A:VAL154 2.6 33.6 1.0 O A:ILE157 2.7 27.5 1.0 O A:ALA152 2.8 29.8 1.0 O A:LYS155 3.2 33.4 1.0 C A:VAL154 3.7 34.0 1.0 C A:ILE157 3.7 28.1 1.0 C A:LYS155 3.7 34.0 1.0 C A:ALA152 3.8 30.3 1.0 CA A:LYS155 4.1 34.5 1.0 N A:ILE157 4.2 30.1 1.0 N A:LYS155 4.3 34.5 1.0 N A:VAL154 4.5 33.7 1.0 CA A:ALA152 4.5 29.5 1.0 CA A:ILE157 4.5 28.8 1.0 N A:ASN156 4.6 33.0 1.0 C A:LYS153 4.6 33.4 1.0 N A:ILE158 4.6 27.4 1.0 CA A:ILE158 4.6 27.1 1.0 CA A:VAL154 4.7 33.9 1.0 N A:LYS153 4.8 31.0 1.0 CG2 A:ILE158 4.9 28.7 1.0 CB A:ILE157 4.9 28.5 1.0 CA A:LYS153 4.9 33.0 1.0 O A:LYS153 4.9 33.9 1.0 CD1 A:PHE181 5.0 29.4 1.0 C A:ASN156 5.0 31.6 1.0

Potassium binding site 2 out of 4 in the Dihydrodipicolinate Synthase Mutant - K161A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Dihydrodipicolinate Synthase Mutant - K161A within 5.0Å range: probe atom residue distance (Å) B Occ A:K296 b:39.3 occ:1.00 O A:LEU51 2.8 23.2 1.0 O A:HOH422 2.8 34.7 1.0 O1 B:GOL293 2.8 25.1 0.5 O A:SER48 2.9 22.9 1.0 O B:HOH450 2.9 30.9 1.0 O A:ALA49 2.9 23.4 1.0 O1 B:GOL293 3.1 23.2 0.5 C A:ALA49 3.5 23.2 1.0 O2 B:GOL293 3.7 25.8 0.5 C A:LEU51 3.8 24.4 1.0 CA A:ALA49 4.0 23.3 1.0 C A:SER48 4.0 22.9 1.0 C1 B:GOL293 4.1 26.3 0.5 N A:LEU51 4.2 24.1 1.0 C1 B:GOL293 4.2 20.4 0.5 N A:THR50 4.3 23.1 1.0 C2 B:GOL293 4.4 25.3 0.5 N A:ALA49 4.5 22.8 1.0 O1 A:GOL294 4.5 28.4 1.0 O2 A:GOL294 4.5 32.0 1.0 CA A:LEU51 4.6 24.5 1.0 N A:ASN52 4.7 24.9 1.0 C A:THR50 4.7 23.7 1.0 CA A:ASN52 4.7 25.4 1.0 CA A:THR50 4.7 23.3 1.0 O B:HOH360 4.9 29.0 1.0 C2 B:GOL293 4.9 21.2 0.5

Potassium binding site 3 out of 4 in the Dihydrodipicolinate Synthase Mutant - K161A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Dihydrodipicolinate Synthase Mutant - K161A within 5.0Å range: probe atom residue distance (Å) B Occ B:K295 b:33.3 occ:1.00 O B:VAL154 2.6 33.9 1.0 O B:ALA152 2.6 29.1 1.0 O B:ILE157 2.6 27.5 1.0 O B:LYS155 3.4 33.1 1.0 C B:VAL154 3.6 34.1 1.0 C B:ALA152 3.7 29.1 1.0 C B:ILE157 3.7 26.9 1.0 C B:LYS155 3.8 33.5 1.0 CA B:LYS155 4.1 34.5 1.0 N B:ILE157 4.2 27.8 1.0 N B:LYS155 4.3 34.4 1.0 CA B:ALA152 4.4 28.4 1.0 N B:VAL154 4.5 33.1 1.0 CA B:ILE157 4.5 27.6 1.0 C B:LYS153 4.6 32.8 1.0 N B:ASN156 4.6 31.6 1.0 N B:ILE158 4.6 26.5 1.0 CA B:ILE158 4.7 26.9 1.0 N B:LYS153 4.7 30.4 1.0 CA B:VAL154 4.7 33.0 1.0 CD1 B:PHE181 4.8 26.5 1.0 CA B:LYS153 4.9 32.3 1.0 CB B:ILE157 4.9 27.2 1.0 O B:LEU151 5.0 26.0 1.0 O B:LYS153 5.0 33.0 1.0

Potassium binding site 4 out of 4 in the Dihydrodipicolinate Synthase Mutant - K161A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Dihydrodipicolinate Synthase Mutant - K161A within 5.0Å range: probe atom residue distance (Å) B Occ B:K296 b:54.7 occ:1.00 O B:HOH310 2.8 39.9 1.0 O B:LEU51 2.8 34.7 1.0 O B:SER48 2.9 26.6 1.0 O B:HOH387 3.0 41.4 1.0 O B:ALA49 3.4 31.1 1.0 C B:ALA49 3.8 30.1 1.0 C B:LEU51 3.9 34.7 1.0 O3 B:GOL293 3.9 23.1 0.5 O3 B:GOL293 4.0 29.2 0.5 C B:SER48 4.1 27.9 1.0 CA B:ALA49 4.2 29.6 1.0 N B:LEU51 4.4 32.3 1.0 N B:THR50 4.5 30.5 1.0 O2 B:GOL294 4.6 36.0 1.0 O1 B:GOL294 4.6 34.5 1.0 N B:ALA49 4.6 28.6 1.0 CA B:ASN52 4.6 37.3 1.0 N B:ASN52 4.7 35.7 1.0 CA B:LEU51 4.8 34.0 1.0 C3 B:GOL293 4.8 27.6 0.5 C3 B:GOL293 4.8 21.4 0.5 O B:HOH430 4.9 25.2 1.0 CD2 B:HIS53 4.9 42.0 1.0

T.P.Soares Da Costa, A.C.Muscroft-Taylor, R.C.Dobson, S.R.Devenish, G.B.Jameson, J.A.Gerrard. How Essential Is the 'Essential' Active-Site Lysine in Dihydrodipicolinate Synthase? Biochimie V. 92 837 2010.
ISSN: ISSN 0300-9084
PubMed: 20353808
DOI: 10.1016/J.BIOCHI.2010.03.004