Potassium in PDB 2dwu: Crystal Structure of Glutamate Racemase Isoform RACE1 From Bacillus Anthracis

All present enzymatic activity of Crystal Structure of Glutamate Racemase Isoform RACE1 From Bacillus Anthracis:
5.1.1.3;

The structure of Crystal Structure of Glutamate Racemase Isoform RACE1 From Bacillus Anthracis, PDB code: 2dwu was solved by S.Mehboob, B.D.Santarsiero, M.E.Johnson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	85.783, 49.659, 198.252, 90.00, 90.07, 90.00
R / Rfree (%)	16.2 / 19.4

The binding sites of Potassium atom in the Crystal Structure of Glutamate Racemase Isoform RACE1 From Bacillus Anthracis (pdb code 2dwu). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Crystal Structure of Glutamate Racemase Isoform RACE1 From Bacillus Anthracis, PDB code: 2dwu:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Crystal Structure of Glutamate Racemase Isoform RACE1 From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Glutamate Racemase Isoform RACE1 From Bacillus Anthracis within 5.0Å range: probe atom residue distance (Å) B Occ A:K277 b:24.5 occ:1.00 OH A:TYR164 2.9 17.9 1.0 CZ A:TYR164 3.8 14.0 1.0 CE2 A:TYR164 3.9 16.2 1.0 NH1 A:ARG158 4.4 15.9 1.0

Potassium binding site 2 out of 3 in the Crystal Structure of Glutamate Racemase Isoform RACE1 From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Glutamate Racemase Isoform RACE1 From Bacillus Anthracis within 5.0Å range: probe atom residue distance (Å) B Occ B:K277 b:24.4 occ:1.00 OD2 B:ASP266 2.8 30.0 1.0 OH C:TYR164 2.9 17.8 1.0 O B:THR242 2.9 13.9 1.0 O B:HOH309 2.9 16.1 1.0 O B:VAL265 3.0 19.3 1.0 O C:HOH396 3.0 28.0 1.0 O B:HOH397 3.3 28.6 1.0 C B:THR242 3.7 12.8 1.0 CA B:THR242 3.8 11.7 1.0 CA B:ASP266 3.8 22.3 1.0 CZ C:TYR164 3.8 15.1 1.0 O C:HOH611 3.8 79.0 1.0 OE2 B:GLU42 3.9 21.0 1.0 CG B:ASP266 3.9 28.5 1.0 CB B:THR242 3.9 10.6 1.0 CE2 C:TYR164 3.9 17.1 1.0 C B:VAL265 3.9 21.4 1.0 OE1 B:GLU42 4.0 20.4 1.0 CD B:GLU42 4.1 20.5 1.0 N B:ASP266 4.3 21.6 1.0 O B:HOH433 4.3 31.0 1.0 O B:HOH408 4.4 30.1 1.0 NH1 C:ARG158 4.4 19.1 1.0 CB B:ASP266 4.4 25.1 1.0 CG2 B:THR242 4.5 12.2 1.0 N B:LEU267 4.8 21.8 1.0 OD1 B:ASP266 4.9 32.0 1.0 C B:ASP266 4.9 23.6 1.0 O B:HOH315 5.0 16.9 1.0

Potassium binding site 3 out of 3 in the Crystal Structure of Glutamate Racemase Isoform RACE1 From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of Glutamate Racemase Isoform RACE1 From Bacillus Anthracis within 5.0Å range: probe atom residue distance (Å) B Occ C:K277 b:24.1 occ:1.00 OD2 C:ASP266 2.9 29.0 1.0 OH B:TYR164 2.9 18.7 1.0 O C:THR242 2.9 13.8 1.0 O B:HOH452 2.9 25.7 1.0 O C:VAL265 2.9 18.4 1.0 O C:HOH313 3.0 17.3 1.0 O C:HOH379 3.4 27.5 1.0 C C:THR242 3.7 13.6 1.0 CZ B:TYR164 3.8 14.9 1.0 OE2 C:GLU42 3.8 21.0 1.0 CA C:THR242 3.8 10.9 1.0 CA C:ASP266 3.9 20.7 1.0 CB C:THR242 3.9 11.3 1.0 C C:VAL265 3.9 19.7 1.0 CE2 B:TYR164 3.9 17.6 1.0 CG C:ASP266 4.0 26.6 1.0 OE1 C:GLU42 4.0 20.0 1.0 CD C:GLU42 4.1 19.3 1.0 N C:ASP266 4.3 19.9 1.0 O C:HOH422 4.3 31.9 1.0 NH2 B:ARG158 4.4 17.0 1.0 O C:HOH455 4.4 35.6 1.0 CB C:ASP266 4.5 23.0 1.0 CG2 C:THR242 4.5 11.3 1.0 N C:LEU267 4.9 20.6 1.0 C C:ASP266 4.9 22.3 1.0 CE1 B:TYR164 5.0 13.2 1.0 N C:GLY243 5.0 14.7 1.0 OD1 C:ASP266 5.0 30.4 1.0

M.May, S.Mehboob, D.C.Mulhearn, Z.Wang, H.Yu, G.R.J.Thatcher, B.D.Santarsiero, M.E.Johnson, A.D.Mesecar. Structural and Functional Analysis of Two Glutamate Racemase Isozymes From Bacillus Anthracis and Implications For Inhibitor Design J.Mol.Biol. V. 371 1219 2007.
ISSN: ISSN 0022-2836
PubMed: 17610893
DOI: 10.1016/J.JMB.2007.05.093