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Chlorine in PDB 6foz: The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13

Enzymatic activity of The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13

All present enzymatic activity of The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13:
1.14.13.9;

Protein crystallography data

The structure of The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13, PDB code: 6foz was solved by C.W.Levy, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 66.89 / 2.15
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 69.540, 52.190, 136.210, 90.00, 103.53, 90.00
R / Rfree (%) 19.9 / 22.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13 (pdb code 6foz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13, PDB code: 6foz:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 6foz

Go back to Chlorine Binding Sites List in 6foz
Chlorine binding site 1 out of 4 in the The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:56.3
occ:1.00
 CL1 A:E0H502 0.0 56.3 1.0
C11 A:E0H502 1.8 50.0 1.0
C13 A:E0H502 2.7 45.3 1.0
C10 A:E0H502 2.7 48.9 1.0
H101 A:E0H502 2.8 58.6 1.0
HZ A:PHE237 2.8 42.1 1.0
H6 A:FAD501 3.0 36.3 1.0
CL2 A:E0H502 3.1 43.0 1.0
HB2 A:PRO317 3.2 37.3 1.0
HE2 A:PHE237 3.2 40.5 1.0
HM72 A:FAD501 3.4 42.8 1.0
C6 A:FAD501 3.5 30.2 1.0
CZ A:PHE237 3.6 35.1 1.0
HG1 A:THR235 3.6 47.5 1.0
HG21 A:THR235 3.7 43.8 1.0
CE2 A:PHE237 3.8 33.8 1.0
HB A:THR235 3.9 46.0 1.0
HG2 A:PRO317 3.9 42.6 1.0
C15 A:E0H502 4.0 46.5 1.0
CB A:PRO317 4.0 31.1 1.0
C09 A:E0H502 4.1 44.9 1.0
HD12 A:ILE223 4.1 60.6 1.0
C5X A:FAD501 4.2 28.7 1.0
C7M A:FAD501 4.2 35.7 1.0
N5 A:FAD501 4.2 25.8 1.0
C7 A:FAD501 4.3 33.6 1.0
HG3 A:PRO317 4.3 42.6 1.0
CG A:PRO317 4.3 35.5 1.0
OG1 A:THR235 4.3 39.6 1.0
CB A:THR235 4.4 38.4 1.0
CG2 A:THR235 4.4 36.5 1.0
HB A:ILE223 4.4 52.8 1.0
HB3 A:PRO317 4.4 37.3 1.0
O A:HOH610 4.5 44.9 1.0
C08 A:E0H502 4.6 47.1 1.0
O A:PRO317 4.6 39.2 1.0
HM73 A:FAD501 4.6 42.8 1.0
HD13 A:ILE223 4.7 60.6 1.0
H151 A:E0H502 4.7 55.8 1.0
HG22 A:THR235 4.8 43.8 1.0
H091 A:E0H502 4.8 53.9 1.0
CD1 A:ILE223 4.8 50.5 1.0
CE1 A:PHE237 4.8 37.4 1.0
HG21 A:ILE223 4.9 53.8 1.0
HM71 A:FAD501 4.9 42.8 1.0
O A:HOH654 5.0 42.5 1.0
C A:PRO317 5.0 37.6 1.0

Chlorine binding site 2 out of 4 in 6foz

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Chlorine binding site 2 out of 4 in the The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:43.0
occ:1.00
 CL2 A:E0H502 0.0 43.0 1.0
C13 A:E0H502 1.8 45.3 1.0
HD12 A:ILE223 2.7 60.6 1.0
C11 A:E0H502 2.7 50.0 1.0
C15 A:E0H502 2.8 46.5 1.0
H151 A:E0H502 2.8 55.8 1.0
HA A:PHE318 3.0 50.0 1.0
HD13 A:ILE223 3.1 60.6 1.0
CL1 A:E0H502 3.1 56.3 1.0
HE2 A:PHE237 3.1 40.5 1.0
CD1 A:ILE223 3.2 50.5 1.0
CD1 A:PHE318 3.4 47.4 1.0
HZ A:PHE237 3.4 42.1 1.0
HD11 A:ILE223 3.4 60.6 1.0
HD1 A:PHE318 3.5 56.8 1.0
CE2 A:PHE237 3.5 33.8 1.0
CE1 A:PHE318 3.7 47.0 1.0
HG2 A:PRO317 3.7 42.6 1.0
CZ A:PHE237 3.7 35.1 1.0
CA A:PHE318 3.8 41.7 1.0
CG A:PHE318 3.8 44.6 1.0
O A:PRO317 3.8 39.2 1.0
HB2 A:PRO317 3.9 37.3 1.0
HE1 A:PHE318 3.9 56.4 1.0
N A:PHE318 3.9 40.1 1.0
C A:PRO317 4.0 37.6 1.0
C10 A:E0H502 4.0 48.9 1.0
C08 A:E0H502 4.1 47.1 1.0
CZ A:PHE318 4.2 48.5 1.0
CB A:PHE318 4.3 43.6 1.0
CD2 A:PHE318 4.3 48.4 1.0
H A:PHE318 4.4 48.1 1.0
O A:HOH633 4.4 45.0 1.0
CG A:PRO317 4.5 35.5 1.0
CE2 A:PHE318 4.5 49.6 1.0
CD2 A:PHE237 4.5 35.1 1.0
CB A:PRO317 4.5 31.1 1.0
C09 A:E0H502 4.6 44.9 1.0
HG21 A:ILE223 4.6 53.8 1.0
HB3 A:PHE318 4.6 52.3 1.0
CG1 A:ILE223 4.6 48.1 1.0
H A:HIS319 4.7 50.3 1.0
HB A:ILE223 4.7 52.8 1.0
H101 A:E0H502 4.7 58.6 1.0
HZ A:PHE318 4.7 58.3 1.0
CE1 A:PHE237 4.8 37.4 1.0
HD2 A:PHE237 4.8 42.1 1.0
CA A:PRO317 4.9 34.0 1.0
HD2 A:PHE318 4.9 58.0 1.0
C A:PHE318 5.0 42.8 1.0

Chlorine binding site 3 out of 4 in 6foz

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Chlorine binding site 3 out of 4 in the The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl502

b:52.0
occ:1.00
 CL1 B:E0H502 0.0 52.0 1.0
C11 B:E0H502 1.8 46.8 1.0
C13 B:E0H502 2.7 43.9 1.0
C10 B:E0H502 2.7 42.8 1.0
H101 B:E0H502 2.8 51.3 1.0
H6 B:FAD501 2.9 39.9 1.0
HB2 B:PRO317 3.0 43.0 1.0
HZ B:PHE237 3.0 47.0 1.0
CL2 B:E0H502 3.1 42.9 1.0
HM72 B:FAD501 3.5 43.7 1.0
C6 B:FAD501 3.5 33.2 1.0
HE2 B:PHE237 3.7 45.1 1.0
HG1 B:THR235 3.7 48.9 1.0
HG21 B:THR235 3.7 41.3 1.0
CZ B:PHE237 3.8 39.2 1.0
HG2 B:PRO317 3.9 46.4 1.0
CB B:PRO317 3.9 35.8 1.0
O B:HOH656 4.0 46.0 1.0
C15 B:E0H502 4.0 42.7 1.0
HB B:THR235 4.0 44.8 1.0
C09 B:E0H502 4.1 43.3 1.0
N5 B:FAD501 4.1 28.5 1.0
C5X B:FAD501 4.1 33.8 1.0
CE2 B:PHE237 4.2 37.6 1.0
CG B:PRO317 4.2 38.7 1.0
HG3 B:PRO317 4.3 46.4 1.0
HB3 B:PRO317 4.3 43.0 1.0
C7M B:FAD501 4.3 36.4 1.0
C7 B:FAD501 4.3 35.8 1.0
HD12 B:ILE223 4.3 57.8 1.0
OG1 B:THR235 4.4 40.7 1.0
O B:PRO317 4.4 39.5 1.0
CG2 B:THR235 4.5 34.4 1.0
HB B:ILE223 4.5 49.0 1.0
CB B:THR235 4.5 37.4 1.0
C08 B:E0H502 4.6 41.7 1.0
HD13 B:ILE223 4.6 57.8 1.0
HM73 B:FAD501 4.7 43.7 1.0
H151 B:E0H502 4.7 51.2 1.0
H091 B:E0H502 4.8 51.9 1.0
HG21 B:ILE223 4.8 50.1 1.0
C B:PRO317 4.8 38.7 1.0
HG22 B:THR235 4.8 41.3 1.0
O B:HOH610 4.9 58.5 1.0
CD1 B:ILE223 5.0 48.1 1.0
HM71 B:FAD501 5.0 43.7 1.0
CA B:PRO317 5.0 35.5 1.0

Chlorine binding site 4 out of 4 in 6foz

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Chlorine binding site 4 out of 4 in the The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 13 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl502

b:42.9
occ:1.00
 CL2 B:E0H502 0.0 42.9 1.0
C13 B:E0H502 1.8 43.9 1.0
HD12 B:ILE223 2.6 57.8 1.0
C11 B:E0H502 2.7 46.8 1.0
C15 B:E0H502 2.8 42.7 1.0
H151 B:E0H502 2.9 51.2 1.0
HD13 B:ILE223 2.9 57.8 1.0
HA B:PHE318 3.0 54.0 1.0
HE2 B:PHE237 3.1 45.1 1.0
CD1 B:ILE223 3.1 48.1 1.0
CL1 B:E0H502 3.1 52.0 1.0
HZ B:PHE237 3.3 47.0 1.0
HD11 B:ILE223 3.4 57.8 1.0
HD1 B:PHE318 3.4 58.5 1.0
CD1 B:PHE318 3.5 48.8 1.0
CE2 B:PHE237 3.5 37.6 1.0
CZ B:PHE237 3.6 39.2 1.0
HG2 B:PRO317 3.7 46.4 1.0
O B:PRO317 3.8 39.5 1.0
CA B:PHE318 3.8 45.0 1.0
CE1 B:PHE318 3.9 48.8 1.0
HB2 B:PRO317 3.9 43.0 1.0
C B:PRO317 4.0 38.7 1.0
HE1 B:PHE318 4.0 58.5 1.0
N B:PHE318 4.0 41.7 1.0
C10 B:E0H502 4.0 42.8 1.0
CG B:PHE318 4.0 47.9 1.0
C08 B:E0H502 4.1 41.7 1.0
HE3 B:MET221 4.2 80.0 1.0
O B:HOH658 4.3 44.0 1.0
CB B:PHE318 4.4 46.7 1.0
HG21 B:ILE223 4.4 50.1 1.0
HB B:ILE223 4.4 49.0 1.0
CG1 B:ILE223 4.5 46.6 1.0
H B:PHE318 4.5 50.0 1.0
C09 B:E0H502 4.6 43.3 1.0
CG B:PRO317 4.6 38.7 1.0
HE1 B:MET221 4.6 80.0 1.0
CB B:PRO317 4.6 35.8 1.0
CD2 B:PHE237 4.6 37.4 1.0
CZ B:PHE318 4.6 50.2 1.0
HB3 B:PHE318 4.6 56.1 1.0
H B:HIS319 4.6 61.3 1.0
CD2 B:PHE318 4.7 49.8 1.0
H101 B:E0H502 4.7 51.3 1.0
CE B:MET221 4.7 66.7 1.0
CE1 B:PHE237 4.8 37.5 1.0
HG13 B:ILE223 4.8 55.9 1.0
HE2 B:MET221 4.9 80.0 1.0
CB B:ILE223 4.9 40.8 1.0
HD2 B:PHE237 4.9 44.9 1.0
CA B:PRO317 4.9 35.5 1.0
H B:GLY320 5.0 47.6 1.0
C B:PHE318 5.0 47.8 1.0
CE2 B:PHE318 5.0 52.0 1.0

Reference:

S.Zhang, M.Sakuma, G.S.Deora, C.W.Levy, A.Klausing, C.Breda, K.Read, C.D.Edlin, B.P.Ross, M.W.Muelas, P.J.Day, S.O'hagan, D.B.Kell, R.Schwarcz, D.Leys, D.J.Heyes, F.Giorgini, N.S.Scrutton. Neuroprotective Brain-Permeable Inhibitors of Kynurenine 3-Monooxygenase To Be Published.
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