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Potassium in PDB 3tz5: Crystal Structure of Branched-Chain Alpha-Ketoacid Dehydrogenase Kinase/Phenylbutyrate Complex with Adp

Enzymatic activity of Crystal Structure of Branched-Chain Alpha-Ketoacid Dehydrogenase Kinase/Phenylbutyrate Complex with Adp

All present enzymatic activity of Crystal Structure of Branched-Chain Alpha-Ketoacid Dehydrogenase Kinase/Phenylbutyrate Complex with Adp:
2.7.11.4;

Protein crystallography data

The structure of Crystal Structure of Branched-Chain Alpha-Ketoacid Dehydrogenase Kinase/Phenylbutyrate Complex with Adp, PDB code: 3tz5 was solved by S.C.Tso, J.L.Chuang, W.J.Gui, R.M.Wynn, J.Li, D.T.Chuang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.52 / 2.40
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 127.703, 127.703, 73.871, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 24

Other elements in 3tz5:

The structure of Crystal Structure of Branched-Chain Alpha-Ketoacid Dehydrogenase Kinase/Phenylbutyrate Complex with Adp also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Branched-Chain Alpha-Ketoacid Dehydrogenase Kinase/Phenylbutyrate Complex with Adp (pdb code 3tz5). 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 Branched-Chain Alpha-Ketoacid Dehydrogenase Kinase/Phenylbutyrate Complex with Adp, PDB code: 3tz5:

Potassium binding site 1 out of 1 in 3tz5

Go back to Potassium Binding Sites List in 3tz5
Potassium binding site 1 out of 1 in the Crystal Structure of Branched-Chain Alpha-Ketoacid Dehydrogenase Kinase/Phenylbutyrate Complex with Adp


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 Branched-Chain Alpha-Ketoacid Dehydrogenase Kinase/Phenylbutyrate Complex with Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K391

b:50.5
occ:1.00
 O A:ASP300 2.9 42.0 1.0
O A:PHE303 2.9 47.5 1.0
O A:VAL298 3.0 42.6 1.0
O2A A:ADP389 3.0 35.5 1.0
O A:GLY337 3.1 41.5 1.0
C5' A:ADP389 3.5 42.0 1.0
C A:GLY337 3.7 49.7 1.0
CD A:PRO341 3.8 35.5 1.0
C A:PHE303 3.8 53.8 1.0
N A:PHE303 3.8 57.3 1.0
CG A:PRO341 3.8 37.9 1.0
C A:VAL298 3.9 41.8 1.0
C A:ASP300 3.9 46.4 1.0
CA A:GLY337 3.9 42.6 1.0
PA A:ADP389 4.0 43.5 1.0
CA A:PHE303 4.0 56.9 1.0
CB A:PHE303 4.0 59.9 1.0
O3A A:ADP389 4.1 55.1 1.0
O5' A:ADP389 4.2 41.4 1.0
N A:ASP300 4.4 35.3 1.0
CA A:VAL298 4.5 55.5 1.0
O A:ARG297 4.6 56.8 1.0
CD2 A:PHE303 4.6 54.0 1.0
N A:PHE338 4.7 41.4 1.0
N A:HIS302 4.7 39.7 1.0
N A:TYR301 4.8 37.3 1.0
C A:MET299 4.8 57.3 1.0
C4' A:ADP389 4.8 48.1 1.0
CA A:ASP300 4.8 42.5 1.0
CB A:LEU340 4.8 36.3 1.0
CA A:TYR301 4.8 43.6 1.0
N A:MET299 4.8 41.4 1.0
C A:HIS302 4.8 63.4 1.0
CG A:PHE303 4.9 59.7 1.0
C A:TYR301 4.9 45.5 1.0
CA A:MET299 5.0 35.2 1.0
N A:THR304 5.0 58.4 1.0

Reference:

S.C.Tso, X.Qi, W.J.Gui, J.L.Chuang, L.K.Morlock, A.L.Wallace, K.Ahmed, S.Laxman, P.M.Campeau, B.H.Lee, S.M.Hutson, B.P.Tu, N.S.Williams, U.K.Tambar, R.M.Wynn, D.T.Chuang. Structure-Based Design and Mechanisms of Allosteric Inhibitors For Mitochondrial Branched-Chain Alpha-Ketoacid Dehydrogenase Kinase. Proc.Natl.Acad.Sci.Usa V. 110 9728 2013.
ISSN: ESSN 1091-6490
PubMed: 23716694
DOI: 10.1073/PNAS.1303220110
Page generated: Mon Aug 12 09:41:15 2024

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