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Potassium in PDB 4tm0: Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadred-Ox-Nadp+-L-Orn

Protein crystallography data

The structure of Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadred-Ox-Nadp+-L-Orn, PDB code: 4tm0 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) 47.16 / 2.74
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 85.029, 156.401, 164.496, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 21.7

Potassium Binding Sites:

The binding sites of Potassium atom in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadred-Ox-Nadp+-L-Orn (pdb code 4tm0). 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-Fadred-Ox-Nadp+-L-Orn, PDB code: 4tm0:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Potassium binding site 1 out of 8 in 4tm0

Go back to Potassium Binding Sites List in 4tm0
Potassium binding site 1 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadred-Ox-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-Fadred-Ox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K504

b:37.6
occ:1.00
 O A:SER33 2.7 20.1 1.0
O A:LEU30 3.0 24.6 1.0
O A:ALA35 3.2 36.8 1.0
O A:GLU31 3.4 24.8 1.0
C A:GLU31 3.9 20.0 1.0
C A:SER33 3.9 23.5 1.0
CA A:GLU31 4.0 17.4 1.0
C A:LEU30 4.0 16.4 1.0
C A:ALA35 4.4 24.9 1.0
N A:GLU31 4.4 18.4 1.0
N A:SER33 4.5 22.1 1.0
CA A:SER33 4.6 18.1 1.0
O A:PRO34 4.7 27.7 1.0
C A:PRO34 4.7 25.2 1.0
N A:GLU32 4.8 16.3 1.0
CB A:SER33 4.9 18.0 1.0
N A:PRO34 4.9 26.6 1.0
C A:GLU32 5.0 18.1 1.0

Potassium binding site 2 out of 8 in 4tm0

Go back to Potassium Binding Sites List in 4tm0
Potassium binding site 2 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadred-Ox-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-Fadred-Ox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K505

b:44.9
occ:1.00
 O A:LEU118 3.0 29.4 1.0
O A:GLU115 3.0 27.0 1.0
O A:HIS120 3.3 36.4 1.0
O A:SER116 3.6 29.2 1.0
O A:HOH645 3.8 14.4 1.0
OE1 A:GLU121 3.8 59.0 1.0
C A:LEU118 4.0 23.7 1.0
C A:SER116 4.1 20.9 1.0
C A:GLU115 4.1 21.8 1.0
CA A:SER116 4.1 20.4 1.0
CD A:GLU121 4.2 52.8 1.0
C A:HIS120 4.3 31.9 1.0
OE2 A:GLU115 4.4 38.6 1.0
CB A:LEU118 4.4 23.8 1.0
CD A:GLU115 4.5 31.9 1.0
N A:SER116 4.5 22.0 1.0
O A:ALA119 4.5 30.6 1.0
CA A:GLU121 4.6 29.7 1.0
OE1 A:GLU115 4.6 29.5 1.0
CA A:LEU118 4.6 25.3 1.0
N A:LEU118 4.7 22.5 1.0
OE2 A:GLU121 4.7 50.0 1.0
CG A:GLU121 4.8 34.6 1.0
C A:ALA119 4.8 25.0 1.0
N A:GLU121 4.9 36.5 1.0

Potassium binding site 3 out of 8 in 4tm0

Go back to Potassium Binding Sites List in 4tm0
Potassium binding site 3 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadred-Ox-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-Fadred-Ox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K504

b:43.5
occ:1.00
 O B:SER33 2.9 29.3 1.0
O B:LEU30 2.9 26.8 1.0
O B:ALA35 3.2 38.8 1.0
O B:GLU31 3.5 36.4 1.0
C B:GLU31 3.9 25.3 1.0
C B:LEU30 3.9 17.9 1.0
CA B:GLU31 4.0 20.7 1.0
C B:SER33 4.0 28.0 1.0
C B:ALA35 4.3 32.0 1.0
N B:GLU31 4.4 17.2 1.0
N B:SER33 4.5 21.4 1.0
CA B:SER33 4.7 23.7 1.0
O B:PRO34 4.8 40.5 1.0
C B:PRO34 4.9 29.6 1.0
N B:GLU32 4.9 20.9 1.0
CA B:ALA36 4.9 40.1 1.0
CB B:SER33 4.9 27.3 1.0

Potassium binding site 4 out of 8 in 4tm0

Go back to Potassium Binding Sites List in 4tm0
Potassium binding site 4 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadred-Ox-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-Fadred-Ox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K505

b:42.0
occ:1.00
 O B:LEU118 2.9 33.0 1.0
O B:GLU115 3.0 33.6 1.0
O B:HIS120 3.1 36.3 1.0
O B:HOH649 3.6 41.0 1.0
O B:SER116 3.6 31.5 1.0
OE1 B:GLU121 3.9 57.1 1.0
C B:LEU118 4.0 28.5 1.0
C B:GLU115 4.0 25.1 1.0
C B:SER116 4.1 23.2 1.0
CA B:SER116 4.2 18.8 1.0
OE1 B:GLU115 4.2 30.6 1.0
C B:HIS120 4.2 34.2 1.0
CD B:GLU121 4.3 58.0 1.0
CB B:LEU118 4.3 27.0 1.0
CD B:GLU115 4.5 31.4 1.0
CA B:LEU118 4.5 27.6 1.0
O B:ALA119 4.5 42.3 1.0
CA B:GLU121 4.5 37.0 1.0
N B:SER116 4.6 24.3 1.0
N B:LEU118 4.6 26.9 1.0
OE2 B:GLU115 4.6 37.1 1.0
OE2 B:GLU121 4.8 54.1 1.0
C B:ALA119 4.8 33.2 1.0
CG B:GLU121 4.8 44.8 1.0
N B:GLU121 4.8 36.0 1.0

Potassium binding site 5 out of 8 in 4tm0

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Potassium binding site 5 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadred-Ox-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-Fadred-Ox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K504

b:63.1
occ:1.00
 O C:SER33 3.0 43.5 1.0
O C:LEU30 3.0 41.7 1.0
O C:ALA35 3.2 54.8 1.0
O C:GLU31 3.6 32.1 1.0
CA C:GLU31 4.0 24.4 1.0
C C:GLU31 4.0 25.1 1.0
C C:LEU30 4.0 31.5 1.0
C C:SER33 4.2 41.0 1.0
C C:ALA35 4.4 48.1 1.0
N C:GLU31 4.5 27.4 1.0
N C:SER33 4.7 33.5 1.0
O C:PRO34 4.7 38.7 1.0
CA C:SER33 4.9 40.9 1.0
C C:PRO34 4.9 43.3 1.0
CA C:ALA36 4.9 66.3 1.0

Potassium binding site 6 out of 8 in 4tm0

Go back to Potassium Binding Sites List in 4tm0
Potassium binding site 6 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadred-Ox-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-Fadred-Ox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K505

b:63.5
occ:1.00
 O C:LEU118 3.0 43.5 1.0
O C:GLU115 3.2 43.4 1.0
O C:SER116 3.4 50.1 1.0
O C:HIS120 3.5 63.7 1.0
C C:SER116 3.9 37.0 1.0
CA C:SER116 4.0 34.3 1.0
C C:LEU118 4.1 38.6 1.0
C C:GLU115 4.2 35.0 1.0
C C:HIS120 4.5 56.4 1.0
O C:ALA119 4.6 45.3 1.0
N C:SER116 4.6 35.3 1.0
OE2 C:GLU115 4.6 37.3 1.0
CB C:LEU118 4.6 31.5 1.0
OE1 C:GLU115 4.7 37.0 1.0
N C:LEU118 4.7 35.0 1.0
CD C:GLU115 4.7 37.2 1.0
CA C:LEU118 4.7 34.7 1.0
CA C:GLU121 4.8 51.9 1.0
C C:ALA119 4.9 39.7 1.0

Potassium binding site 7 out of 8 in 4tm0

Go back to Potassium Binding Sites List in 4tm0
Potassium binding site 7 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadred-Ox-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-Fadred-Ox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K504

b:48.6
occ:1.00
 O D:LEU30 2.9 29.1 1.0
O D:SER33 3.0 41.5 1.0
O D:ALA35 3.2 42.9 1.0
O D:GLU31 3.5 28.7 1.0
C D:LEU30 3.9 21.4 1.0
C D:GLU31 3.9 22.0 1.0
CA D:GLU31 3.9 15.4 1.0
C D:SER33 4.1 30.9 1.0
C D:ALA35 4.3 40.4 1.0
N D:GLU31 4.4 17.5 1.0
N D:SER33 4.6 24.7 1.0
O D:PRO34 4.8 43.2 1.0
CA D:SER33 4.8 25.5 1.0
CA D:ALA36 4.9 46.5 1.0
C D:PRO34 4.9 38.2 1.0
N D:GLU32 4.9 20.7 1.0

Potassium binding site 8 out of 8 in 4tm0

Go back to Potassium Binding Sites List in 4tm0
Potassium binding site 8 out of 8 in the Kutzneria Sp. 744 Ornithine N-Hydroxylase, Ktzi-Fadred-Ox-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-Fadred-Ox-Nadp+-L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K505

b:47.8
occ:1.00
 O D:LEU118 2.7 39.8 1.0
O D:HOH642 2.8 34.9 1.0
O D:GLU115 3.0 32.4 1.0
O D:HIS120 3.0 48.0 1.0
C D:LEU118 3.6 37.0 1.0
O D:SER116 3.7 36.3 1.0
C D:HIS120 3.9 45.7 1.0
CB D:LEU118 4.0 28.8 1.0
OE1 D:GLU121 4.0 64.0 1.0
C D:GLU115 4.1 29.0 1.0
O D:ALA119 4.1 41.5 1.0
C D:SER116 4.2 29.5 1.0
CA D:LEU118 4.2 30.5 1.0
CA D:SER116 4.3 24.5 1.0
C D:ALA119 4.3 40.2 1.0
CA D:GLU121 4.4 44.0 1.0
CD D:GLU121 4.4 64.2 1.0
N D:LEU118 4.4 31.4 1.0
CG D:GLU121 4.5 50.7 1.0
N D:GLU121 4.5 44.4 1.0
N D:ALA119 4.6 41.5 1.0
N D:SER116 4.7 27.0 1.0
OE2 D:GLU115 4.7 38.0 1.0
N D:HIS120 4.7 40.8 1.0
CD D:GLU115 4.8 25.6 1.0
CA D:ALA119 4.8 37.7 1.0
OE1 D:GLU115 4.9 29.9 1.0
CG D:LEU118 4.9 28.1 1.0
CA D:HIS120 5.0 41.7 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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