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Potassium in PDB 4tlz: Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn

Protein crystallography data

The structure of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn, PDB code: 4tlz was solved by J.W.Setser, C.L.Drennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.30 / 2.41
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 84.620, 157.660, 165.293, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 21.5

Potassium Binding Sites:

The binding sites of Potassium atom in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn (pdb code 4tlz). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 8 binding sites of Potassium where determined in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn, PDB code: 4tlz:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Potassium binding site 1 out of 8 in 4tlz

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Potassium binding site 1 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K504

b:48.2
occ:1.00
 O A:SER33 2.7 28.2 1.0
O A:LEU30 3.0 24.7 1.0
O A:ALA35 3.3 38.2 1.0
O A:GLU31 3.4 27.3 1.0
O A:HOH736 3.6 29.1 1.0
C A:SER33 3.9 28.6 1.0
C A:GLU31 3.9 24.8 1.0
CA A:GLU31 4.0 23.9 1.0
C A:LEU30 4.0 23.1 1.0
C A:ALA35 4.4 38.5 1.0
N A:SER33 4.5 27.7 1.0
N A:GLU31 4.5 23.8 1.0
CA A:SER33 4.6 26.4 1.0
C A:PRO34 4.7 30.7 1.0
O A:PRO34 4.7 34.4 1.0
N A:GLU32 4.8 25.7 1.0
N A:PRO34 4.9 24.5 1.0
CB A:SER33 4.9 25.9 1.0
CA A:PRO34 5.0 32.5 1.0
N A:ALA35 5.0 30.7 1.0
C A:GLU32 5.0 27.0 1.0

Potassium binding site 2 out of 8 in 4tlz

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Potassium binding site 2 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K505

b:40.0
occ:1.00
 O A:LEU118 2.8 34.2 1.0
O A:GLU115 2.8 31.2 1.0
O A:HOH650 2.9 36.5 1.0
O A:HIS120 3.0 40.8 1.0
O A:SER116 3.6 31.9 1.0
OE1 A:GLU121 3.8 55.3 1.0
C A:LEU118 3.8 33.0 1.0
K A:K506 3.9 79.0 1.0
C A:GLU115 3.9 27.7 1.0
CB A:LEU118 4.0 29.2 1.0
C A:HIS120 4.1 33.6 1.0
C A:SER116 4.1 24.3 1.0
CA A:SER116 4.2 30.7 1.0
CA A:LEU118 4.3 32.2 1.0
CD A:GLU121 4.3 56.0 1.0
OE2 A:GLU115 4.4 41.4 1.0
O A:ALA119 4.4 36.6 1.0
N A:LEU118 4.4 26.0 1.0
CA A:GLU121 4.5 30.2 1.0
N A:SER116 4.5 25.0 1.0
CD A:GLU115 4.5 33.5 1.0
OE2 A:GLU121 4.6 60.5 1.0
C A:ALA119 4.6 32.5 1.0
OE1 A:GLU115 4.6 31.8 1.0
N A:GLU121 4.7 33.8 1.0
N A:ALA119 4.9 31.3 1.0
CG A:LEU118 4.9 31.9 1.0
N A:HIS120 5.0 32.6 1.0

Potassium binding site 3 out of 8 in 4tlz

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Potassium binding site 3 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K506

b:79.0
occ:1.00
 O A:SER116 2.6 31.9 1.0
O A:LEU118 2.9 34.2 1.0
C A:LEU118 3.8 33.0 1.0
C A:SER116 3.8 24.3 1.0
K A:K505 3.9 40.0 1.0
O A:LYS117 4.0 29.5 1.0
C A:LYS117 4.1 26.8 1.0
CA A:ALA119 4.4 31.8 1.0
N A:ALA119 4.5 31.3 1.0
N A:LEU118 4.5 26.0 1.0
O A:ALA119 4.5 36.6 1.0
CA A:LYS117 4.5 25.0 1.0
N A:LYS117 4.6 24.5 1.0
CA A:LEU118 4.8 32.2 1.0
C A:ALA119 4.8 32.5 1.0
CA A:SER116 4.9 30.7 1.0

Potassium binding site 4 out of 8 in 4tlz

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Potassium binding site 4 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K504

b:47.1
occ:1.00
 O B:SER33 2.6 34.7 1.0
O B:LEU30 2.8 23.4 1.0
O B:ALA35 3.1 36.1 1.0
O B:GLU31 3.4 26.3 1.0
C B:SER33 3.7 28.3 1.0
C B:GLU31 3.9 24.9 1.0
C B:LEU30 3.9 19.4 1.0
CA B:GLU31 4.0 21.3 1.0
C B:ALA35 4.2 36.6 1.0
N B:SER33 4.3 24.5 1.0
N B:GLU31 4.4 20.2 1.0
CA B:SER33 4.5 25.7 1.0
C B:PRO34 4.6 37.8 1.0
O B:PRO34 4.6 40.8 1.0
CB B:SER33 4.6 26.4 1.0
N B:PRO34 4.7 29.8 1.0
N B:GLU32 4.8 23.8 1.0
N B:ALA35 4.8 32.4 1.0
CA B:PRO34 4.9 35.1 1.0
C B:GLU32 4.9 24.5 1.0

Potassium binding site 5 out of 8 in 4tlz

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Potassium binding site 5 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K505

b:55.9
occ:1.00
 O B:HOH610 2.9 49.5 1.0
O B:LEU118 3.0 39.0 1.0
O B:GLU115 3.0 30.5 1.0
O B:HOH703 3.1 37.3 1.0
O B:HIS120 3.4 46.7 1.0
O B:SER116 3.5 37.2 1.0
CA B:SER116 4.0 25.0 1.0
C B:SER116 4.0 27.9 1.0
C B:GLU115 4.0 30.4 1.0
CG B:GLU121 4.1 55.3 1.0
C B:LEU118 4.1 33.3 1.0
OE2 B:GLU115 4.3 40.9 1.0
CB B:LEU118 4.4 31.1 1.0
N B:SER116 4.5 26.6 1.0
C B:HIS120 4.5 37.7 1.0
CD B:GLU115 4.5 39.2 1.0
OE1 B:GLU115 4.6 37.9 1.0
OE1 B:GLU121 4.6 75.8 1.0
N B:LEU118 4.6 29.2 1.0
CA B:LEU118 4.6 30.6 1.0
O B:ALA119 4.6 55.0 1.0
CA B:GLU121 4.7 38.8 1.0
CD B:GLU121 4.9 64.9 1.0
C B:ALA119 5.0 46.6 1.0

Potassium binding site 6 out of 8 in 4tlz

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Potassium binding site 6 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K504

b:64.8
occ:1.00
 O C:SER33 2.9 48.1 1.0
O C:LEU30 3.0 41.5 1.0
O C:GLU31 3.4 38.2 1.0
O C:ALA35 3.4 62.6 1.0
C C:GLU31 3.9 35.7 1.0
CA C:GLU31 4.0 33.7 1.0
C C:SER33 4.1 50.4 1.0
C C:LEU30 4.1 40.0 1.0
N C:GLU31 4.5 37.6 1.0
C C:ALA35 4.5 62.0 1.0
N C:SER33 4.6 33.1 1.0
O C:PRO34 4.8 62.0 1.0
CA C:SER33 4.8 48.3 1.0
C C:PRO34 4.8 59.8 1.0
N C:GLU32 4.9 34.9 1.0

Potassium binding site 7 out of 8 in 4tlz

Go back to Potassium Binding Sites List in 4tlz
Potassium binding site 7 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 7 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K505

b:60.0
occ:1.00
 O C:HIS120 3.0 60.5 1.0
O C:GLU115 3.0 40.6 1.0
O C:LEU118 3.0 45.9 1.0
O C:HOH714 3.5 42.4 1.0
OE1 C:GLU121 3.5 72.6 1.0
O C:SER116 3.8 47.9 1.0
CD C:GLU121 4.0 71.9 1.0
C C:LEU118 4.0 46.8 1.0
C C:HIS120 4.1 52.9 1.0
C C:GLU115 4.1 41.9 1.0
OE2 C:GLU115 4.2 50.1 1.0
CA C:SER116 4.3 37.5 1.0
C C:SER116 4.3 42.1 1.0
OE2 C:GLU121 4.3 74.4 1.0
CB C:LEU118 4.3 41.2 1.0
CA C:GLU121 4.3 48.2 1.0
CD C:GLU115 4.4 43.8 1.0
O C:ALA119 4.5 43.6 1.0
OE1 C:GLU115 4.6 43.1 1.0
CA C:LEU118 4.6 39.3 1.0
N C:SER116 4.6 38.2 1.0
N C:GLU121 4.7 49.3 1.0
N C:LEU118 4.7 36.7 1.0
C C:ALA119 4.8 49.6 1.0

Potassium binding site 8 out of 8 in 4tlz

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Potassium binding site 8 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 8 of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K504

b:54.3
occ:1.00
 O D:SER33 2.8 37.8 1.0
O D:LEU30 3.0 32.8 1.0
O D:GLU31 3.3 34.0 1.0
O D:ALA35 3.4 48.2 1.0
C D:GLU31 3.8 33.5 1.0
CA D:GLU31 3.9 30.4 1.0
C D:SER33 4.0 35.2 1.0
C D:LEU30 4.0 29.9 1.0
N D:GLU31 4.5 30.2 1.0
C D:ALA35 4.5 44.6 1.0
N D:SER33 4.5 34.1 1.0
CA D:SER33 4.7 33.1 1.0
O D:PRO34 4.8 41.8 1.0
C D:PRO34 4.8 43.1 1.0
N D:GLU32 4.8 34.8 1.0
N D:PRO34 5.0 42.8 1.0
CB D:SER33 5.0 32.7 1.0

Reference:

J.W.Setser, J.R.Heemstra, C.T.Walsh, C.L.Drennan. Crystallographic Evidence For Drastic Conformational Changes in the Active Site of A Flavin-Dependent N-Hydroxylase. Biochemistry 2014.
ISSN: ISSN 0006-2960
PubMed: 25184411
DOI: 10.1021/BI500655Q
Page generated: Mon Aug 12 12:06:36 2024

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