Potassium in PDB 3ven: Crystal Structure of the O-Carbamoyltransferase Tobz

The structure of Crystal Structure of the O-Carbamoyltransferase Tobz, PDB code: 3ven was solved by C.Parthier, M.T.Stubbs, S.Goerlich, F.Jaenecke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.09 / 1.57
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	99.023, 99.023, 280.896, 90.00, 90.00, 120.00
R / Rfree (%)	14.4 / 17.6

The structure of Crystal Structure of the O-Carbamoyltransferase Tobz also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Potassium atom in the Crystal Structure of the O-Carbamoyltransferase Tobz (pdb code 3ven). 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 the O-Carbamoyltransferase Tobz, PDB code: 3ven:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Crystal Structure of the O-Carbamoyltransferase Tobz


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 the O-Carbamoyltransferase Tobz within 5.0Å range: probe atom residue distance (Å) B Occ A:K601 b:21.4 occ:0.69 O A:THR565 2.7 26.9 1.0 O A:HOH728 3.0 21.2 1.0 OG1 A:THR565 3.2 29.7 1.0 O A:HOH1268 3.2 31.7 1.0 O A:LYS566 3.5 36.1 1.0 C A:THR565 3.6 23.1 1.0 O A:HOH1295 3.7 45.7 1.0 C A:LYS566 3.8 35.5 1.0 CA A:ASP567 3.8 32.3 0.7 O A:HOH1233 3.9 26.9 1.0 N A:ASP567 4.0 32.7 0.7 CA A:THR565 4.2 18.9 1.0 N A:THR565 4.2 18.1 1.0 CB A:THR565 4.2 23.5 1.0 CB A:ASP567 4.4 37.2 0.7 N A:LYS566 4.5 25.9 1.0 CA A:LYS566 4.7 31.5 1.0 CG A:ASP567 4.8 38.9 0.7 O A:ALA385 4.8 24.3 1.0 OD1 A:ASP567 4.9 41.0 0.7

Potassium binding site 2 out of 3 in the Crystal Structure of the O-Carbamoyltransferase Tobz


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 the O-Carbamoyltransferase Tobz within 5.0Å range: probe atom residue distance (Å) B Occ A:K602 b:27.5 occ:1.00 O A:VAL327 2.7 26.2 1.0 O A:ARG324 2.8 26.5 1.0 O A:LEU322 2.8 23.0 1.0 O A:HOH1001 3.1 41.6 1.0 O A:HOH1351 3.5 53.0 1.0 C A:THR323 3.7 21.1 1.0 C A:ARG324 3.7 25.1 1.0 O A:THR323 3.8 24.6 1.0 C A:LEU322 3.9 21.8 1.0 C A:VAL327 3.9 24.5 1.0 N A:ARG324 3.9 22.5 1.0 CA A:THR323 4.0 24.3 1.0 N A:THR323 4.4 21.7 1.0 CA A:ARG324 4.4 22.7 1.0 CB A:VAL327 4.6 22.1 1.0 N A:VAL327 4.6 21.4 1.0 N A:SER325 4.6 24.0 1.0 CA A:VAL327 4.7 21.5 1.0 CA A:SER325 4.7 24.8 1.0 CA A:ASP328 4.8 23.6 1.0 N A:ASP328 4.8 22.0 1.0 O A:HOH1053 4.9 37.8 1.0 C A:SER325 5.0 23.9 1.0

Potassium binding site 3 out of 3 in the Crystal Structure of the O-Carbamoyltransferase Tobz


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 the O-Carbamoyltransferase Tobz within 5.0Å range: probe atom residue distance (Å) B Occ A:K603 b:31.4 occ:0.84 O A:HOH1383 2.7 46.3 1.0 O A:TYR245 2.9 21.6 1.0 O A:GLU242 3.0 20.0 1.0 O A:ARG243 3.1 26.5 0.5 O A:ARG243 3.1 27.1 0.5 O A:HOH1207 3.2 50.8 1.0 O A:HOH732 3.5 21.2 1.0 O A:HOH1019 3.5 51.0 1.0 O A:HOH1353 3.6 54.2 1.0 C A:ARG243 3.7 21.6 0.5 C A:ARG243 3.7 21.7 0.5 C A:TYR245 3.8 22.1 1.0 C A:GLU242 4.1 17.6 1.0 N A:TYR245 4.2 20.5 1.0 O A:HOH1266 4.3 25.6 1.0 CA A:ARG243 4.3 21.8 0.5 CA A:ARG243 4.3 21.8 0.5 N A:ILE244 4.3 19.7 1.0 C A:ILE244 4.4 22.2 1.0 CA A:ARG246 4.4 20.2 1.0 N A:ARG246 4.5 20.3 1.0 CA A:TYR245 4.6 19.7 1.0 N A:ARG243 4.7 18.8 0.5 N A:ARG243 4.7 18.7 0.5 CA A:ILE244 4.7 21.3 1.0 C A:ARG246 4.8 19.2 1.0 O A:ARG246 4.8 21.4 1.0 O A:HOH1107 4.8 40.7 1.0 O A:ILE244 4.9 28.2 1.0

C.Parthier, S.Gorlich, F.Jaenecke, C.Breithaupt, U.Brauer, U.Fandrich, D.Clausnitzer, U.F.Wehmeier, C.Bottcher, D.Scheel, M.T.Stubbs. The O-Carbamoyltransferase Tobz Catalyzes An Ancient Enzymatic Reaction. Angew.Chem.Int.Ed.Engl. V. 51 4046 2012.
ISSN: ISSN 1433-7851
PubMed: 22383337
DOI: 10.1002/ANIE.201108896