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Potassium in PDB 3rte: Crystal Structure of TM0922, A Fusion of A Domain of Unknown Function and Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Thermotoga Maritima Soaked with Nadp and Atp.

Enzymatic activity of Crystal Structure of TM0922, A Fusion of A Domain of Unknown Function and Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Thermotoga Maritima Soaked with Nadp and Atp.

All present enzymatic activity of Crystal Structure of TM0922, A Fusion of A Domain of Unknown Function and Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Thermotoga Maritima Soaked with Nadp and Atp.:
4.2.1.93;

Protein crystallography data

The structure of Crystal Structure of TM0922, A Fusion of A Domain of Unknown Function and Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Thermotoga Maritima Soaked with Nadp and Atp., PDB code: 3rte was solved by I.A.Shumilin, M.Cymborowski, S.A.Lesley, W.Minor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.10
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 122.441, 122.441, 155.050, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 20.7

Other elements in 3rte:

The structure of Crystal Structure of TM0922, A Fusion of A Domain of Unknown Function and Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Thermotoga Maritima Soaked with Nadp and Atp. also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of TM0922, A Fusion of A Domain of Unknown Function and Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Thermotoga Maritima Soaked with Nadp and Atp. (pdb code 3rte). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of TM0922, A Fusion of A Domain of Unknown Function and Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Thermotoga Maritima Soaked with Nadp and Atp., PDB code: 3rte:

Potassium binding site 1 out of 1 in 3rte

Go back to Potassium Binding Sites List in 3rte
Potassium binding site 1 out of 1 in the Crystal Structure of TM0922, A Fusion of A Domain of Unknown Function and Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Thermotoga Maritima Soaked with Nadp and Atp.


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 TM0922, A Fusion of A Domain of Unknown Function and Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Thermotoga Maritima Soaked with Nadp and Atp. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K491

b:33.9
occ:1.00
 O A:VAL148 2.7 31.5 1.0
O A:PHE117 2.7 31.7 1.0
O A:VAL146 2.8 27.7 1.0
OD1 A:ASN52 2.8 29.0 1.0
O A:ASP114 3.0 30.2 1.0
OG A:SER150 3.0 30.2 1.0
OD2 A:ASP114 3.4 29.1 1.0
C A:PHE117 3.6 32.7 1.0
CG A:ASP114 3.6 30.5 1.0
OD1 A:ASP114 3.7 27.3 1.0
CG A:ASN52 3.7 28.3 1.0
N A:SER150 3.8 31.7 1.0
C A:VAL146 3.8 26.8 1.0
C A:ASP114 3.9 29.2 1.0
C A:VAL148 3.9 31.8 1.0
ND2 A:ASN52 4.0 25.6 1.0
N A:VAL146 4.0 28.0 1.0
N A:PHE117 4.1 32.1 1.0
N A:ILE116 4.1 31.1 1.0
CA A:ALA115 4.1 29.9 1.0
CB A:SER150 4.2 32.3 1.0
CA A:SER150 4.2 31.1 1.0
CA A:VAL146 4.4 26.8 1.0
N A:GLY118 4.4 33.4 1.0
C A:PRO149 4.4 32.3 1.0
N A:ALA115 4.4 30.9 1.0
C A:ALA115 4.4 30.7 1.0
CA A:PHE117 4.5 33.3 1.0
N A:VAL148 4.5 30.5 1.0
CA A:GLY118 4.5 33.0 1.0
CA A:PRO149 4.5 32.5 1.0
CB A:VAL146 4.5 26.8 1.0
CB A:ASP114 4.7 29.9 1.0
N A:PRO149 4.7 31.5 1.0
CB A:SER145 4.8 29.9 1.0
C A:SER145 4.8 29.0 1.0
C A:ILE116 4.9 32.2 1.0
CA A:VAL148 4.9 32.3 1.0
CA A:ASP114 4.9 29.8 1.0
CA A:SER145 5.0 29.2 1.0
OG A:SER145 5.0 29.1 1.0
N A:ASP147 5.0 28.4 1.0
CA A:ILE116 5.0 31.7 1.0

Reference:

I.A.Shumilin, M.Cymborowski, O.Chertihin, K.N.Jha, J.C.Herr, S.A.Lesley, A.Joachimiak, W.Minor. Identification of Unknown Protein Function Using Metabolite Cocktail Screening. Structure V. 20 1715 2012.
ISSN: ISSN 0969-2126
PubMed: 22940582
DOI: 10.1016/J.STR.2012.07.016
Page generated: Mon Aug 12 09:23:32 2024

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