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Potassium in PDB 1uc5: Structure of Diol Dehydratase Complexed with (R)-1,2- Propanediol

Enzymatic activity of Structure of Diol Dehydratase Complexed with (R)-1,2- Propanediol

All present enzymatic activity of Structure of Diol Dehydratase Complexed with (R)-1,2- Propanediol:
4.2.1.28;

Protein crystallography data

The structure of Structure of Diol Dehydratase Complexed with (R)-1,2- Propanediol, PDB code: 1uc5 was solved by N.Shibata, Y.Nakanishi, M.Fukuoka, M.Yamanishi, N.Yasuoka, T.Toraya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.85 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 74.640, 122.270, 207.430, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 25.5

Other elements in 1uc5:

The structure of Structure of Diol Dehydratase Complexed with (R)-1,2- Propanediol also contains other interesting chemical elements:

Cobalt (Co) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Diol Dehydratase Complexed with (R)-1,2- Propanediol (pdb code 1uc5). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of Diol Dehydratase Complexed with (R)-1,2- Propanediol, PDB code: 1uc5:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1uc5

Go back to Potassium Binding Sites List in 1uc5
Potassium binding site 1 out of 2 in the Structure of Diol Dehydratase Complexed with (R)-1,2- Propanediol


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Diol Dehydratase Complexed with (R)-1,2- Propanediol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1603

b:26.5
occ:1.00
O A:SER362 2.1 26.5 1.0
OE1 A:GLU170 2.3 27.1 1.0
OE1 A:GLN296 2.3 23.4 1.0
OE1 A:GLU221 2.4 31.9 1.0
OE1 A:GLN141 2.4 30.5 1.0
O2 A:PGR1602 2.5 25.2 1.0
O1 A:PGR1602 2.6 27.5 1.0
C A:SER362 3.3 27.5 1.0
C1 A:PGR1602 3.3 26.8 1.0
CD A:GLN296 3.3 25.6 1.0
CD A:GLU221 3.3 30.2 1.0
CD A:GLU170 3.4 27.5 1.0
C2 A:PGR1602 3.4 27.8 1.0
CD A:GLN141 3.5 26.1 1.0
OE2 A:GLU221 3.7 31.2 1.0
OE2 A:GLU170 3.7 26.0 1.0
NE2 A:GLN296 3.9 25.3 1.0
CB A:SER362 3.9 28.0 1.0
NE2 A:GLN141 3.9 26.6 1.0
OG A:SER362 4.0 31.4 1.0
OD2 A:ASP335 4.0 28.4 1.0
NE2 A:HIS143 4.1 25.8 1.0
CA A:SER362 4.1 27.0 1.0
N A:GLY363 4.2 27.9 1.0
CA A:GLY363 4.4 28.2 1.0
NE2 A:GLN200 4.4 25.4 1.0
CD2 A:HIS143 4.5 28.9 1.0
CG A:GLN296 4.6 27.0 1.0
CG A:GLU221 4.6 31.1 1.0
CG A:GLU170 4.6 27.2 1.0
C3 A:PGR1602 4.7 29.4 1.0
CG A:GLN141 4.8 25.6 1.0
CB A:GLU170 4.9 29.7 1.0
CG A:ASP335 4.9 27.2 1.0

Potassium binding site 2 out of 2 in 1uc5

Go back to Potassium Binding Sites List in 1uc5
Potassium binding site 2 out of 2 in the Structure of Diol Dehydratase Complexed with (R)-1,2- Propanediol


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of Diol Dehydratase Complexed with (R)-1,2- Propanediol within 5.0Å range:
probe atom residue distance (Å) B Occ
L:K2603

b:27.5
occ:1.00
O L:SER362 2.2 26.1 1.0
O2 L:PGR2602 2.3 20.0 1.0
OE1 L:GLU221 2.4 34.6 1.0
OE1 L:GLU170 2.4 34.5 1.0
OE1 L:GLN141 2.5 29.8 1.0
O1 L:PGR2602 2.6 27.7 1.0
OE1 L:GLN296 2.7 26.0 1.0
C L:SER362 3.3 26.3 1.0
C2 L:PGR2602 3.3 24.0 1.0
CD L:GLU170 3.3 34.5 1.0
C1 L:PGR2602 3.4 22.5 1.0
CD L:GLU221 3.4 32.2 1.0
CD L:GLN296 3.5 26.4 1.0
CD L:GLN141 3.6 32.5 1.0
OE2 L:GLU170 3.6 32.7 1.0
OE2 L:GLU221 3.9 30.9 1.0
NE2 L:GLN296 3.9 25.3 1.0
CB L:SER362 3.9 24.2 1.0
NE2 L:HIS143 4.0 36.4 1.0
OG L:SER362 4.0 25.5 1.0
NE2 L:GLN141 4.1 33.6 1.0
CA L:SER362 4.1 25.3 1.0
OD2 L:ASP335 4.2 29.9 1.0
N L:GLY363 4.2 27.6 1.0
CA L:GLY363 4.4 29.2 1.0
NE2 L:GLN200 4.4 35.5 1.0
CD2 L:HIS143 4.4 35.3 1.0
CG L:GLU221 4.6 32.4 1.0
C3 L:PGR2602 4.6 20.4 1.0
CG L:GLN296 4.7 25.8 1.0
CG L:GLU170 4.7 33.6 1.0
CG L:GLN141 4.9 31.6 1.0
CB L:GLU170 4.9 32.2 1.0

Reference:

N.Shibata, Y.Nakanishi, M.Fukuoka, M.Yamanishi, N.Yasuoka, T.Toraya. Structural Rationalization For the Lack of Stereospecificity in Coenzyme B12-Dependent Diol Dehydratase J.Biol.Chem. V. 278 22717 2003.
ISSN: ISSN 0021-9258
PubMed: 12684496
DOI: 10.1074/JBC.M301513200
Page generated: Mon Aug 12 05:34:18 2024

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