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Chlorine in PDB 6fp1: The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 1

Enzymatic activity of The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 1

All present enzymatic activity of The Crystal Structure of P.Fluorescens Kynurenine 3-Monooxygenase (Kmo) in Complex with Competitive Inhibitor No. 1:
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. 1, PDB code: 6fp1 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) 19.98 / 1.97
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 71.080, 52.920, 137.460, 90.00, 104.08, 90.00
R / Rfree (%) 18.2 / 21.2

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. 1 (pdb code 6fp1). 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. 1, PDB code: 6fp1:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 6fp1

Go back to Chlorine Binding Sites List in 6fp1
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. 1


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. 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:23.2
occ:1.00
 H A:GLY322 2.3 22.8 1.0
HA A:PRO317 2.5 24.4 1.0
H A:GLN321 2.8 23.5 1.0
O A:HOH676 3.1 22.5 1.0
N A:GLY322 3.1 19.0 1.0
H1'2 A:FAD501 3.1 22.2 1.0
O A:HOH648 3.3 20.5 1.0
C10 A:FAD501 3.3 18.7 1.0
HA3 A:GLY322 3.3 23.9 1.0
HA2 A:GLY320 3.3 22.5 1.0
N10 A:FAD501 3.3 18.3 1.0
CA A:PRO317 3.4 20.3 1.0
N A:GLN321 3.4 19.6 1.0
N1 A:FAD501 3.4 17.2 1.0
H A:GLY320 3.4 20.9 1.0
HB3 A:PRO317 3.6 24.3 1.0
C1' A:FAD501 3.6 18.5 1.0
CA A:GLY322 3.7 19.9 1.0
O A:PRO317 3.8 19.4 1.0
H1'1 A:FAD501 3.8 22.2 1.0
C4X A:FAD501 3.9 20.6 1.0
CA A:GLY320 3.9 18.8 1.0
CB A:PRO317 3.9 20.2 1.0
N A:GLY320 3.9 17.5 1.0
C A:PRO317 3.9 21.2 1.0
C A:GLY320 3.9 20.3 1.0
C9A A:FAD501 4.0 22.2 1.0
HB2 A:PRO317 4.0 24.3 1.0
HG3 A:MET315 4.0 29.5 1.0
C2 A:FAD501 4.1 16.5 1.0
C A:GLN321 4.1 19.5 1.0
O A:VAL316 4.2 21.7 1.0
HA2 A:GLY322 4.2 23.9 1.0
CA A:GLN321 4.3 19.1 1.0
N5 A:FAD501 4.4 20.3 1.0
C5X A:FAD501 4.4 22.3 1.0
N A:PRO317 4.4 21.7 1.0
H A:MET323 4.5 21.6 0.5
HG2 A:MET315 4.5 29.5 1.0
H A:MET323 4.5 21.6 0.5
C4 A:FAD501 4.5 18.7 1.0
H A:HIS319 4.5 23.0 1.0
N3 A:FAD501 4.6 17.8 1.0
CG A:MET315 4.6 24.6 1.0
C A:VAL316 4.7 22.8 1.0
C9 A:FAD501 4.7 23.7 1.0
HA3 A:GLY320 4.8 22.5 1.0
O2 A:FAD501 4.8 16.6 1.0
SD A:MET315 4.8 24.3 1.0
HB2 A:GLN321 4.9 22.3 1.0
C A:GLY322 5.0 19.0 1.0
HA A:GLN321 5.0 22.9 1.0

Chlorine binding site 2 out of 4 in 6fp1

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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. 1


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. 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl504

b:25.2
occ:1.00
 CL9 A:E0Q504 0.0 25.2 1.0
C08 A:E0Q504 1.8 26.3 1.0
H073 A:E0Q504 2.5 32.8 1.0
C06 A:E0Q504 2.7 27.2 1.0
C02 A:E0Q504 2.7 26.6 1.0
HD13 A:ILE223 2.9 38.0 1.0
H011 A:E0Q504 2.9 33.7 1.0
C07 A:E0Q504 2.9 27.3 1.0
HA A:PHE318 3.1 28.4 1.0
HD1 A:PHE318 3.1 35.4 1.0
C01 A:E0Q504 3.1 28.1 1.0
HG21 A:ILE223 3.2 31.9 1.0
H012 A:E0Q504 3.2 33.7 1.0
H071 A:E0Q504 3.3 32.8 1.0
HE1 A:MET221 3.3 41.9 1.0
HE2 A:PHE237 3.5 25.1 1.0
HE3 A:MET221 3.5 41.9 1.0
H072 A:E0Q504 3.8 32.8 1.0
CD1 A:ILE223 3.8 31.7 1.0
CE A:MET221 3.8 34.9 1.0
CD1 A:PHE318 4.0 29.5 1.0
CE2 A:PHE237 4.0 20.9 1.0
C03 A:E0Q504 4.0 27.0 1.0
H013 A:E0Q504 4.0 33.7 1.0
CA A:PHE318 4.0 23.6 1.0
C05 A:E0Q504 4.1 28.4 1.0
CG2 A:ILE223 4.1 26.6 1.0
O A:PRO317 4.2 19.4 1.0
HZ A:PHE237 4.2 25.2 1.0
HG23 A:ILE223 4.2 31.9 1.0
HD11 A:ILE223 4.2 38.0 1.0
HE2 A:MET221 4.2 41.9 1.0
HD12 A:ILE223 4.3 38.0 1.0
CZ A:PHE237 4.4 21.1 1.0
HG12 A:ILE223 4.5 35.9 1.0
O A:PHE318 4.5 25.0 1.0
C04 A:E0Q504 4.5 28.0 1.0
HB3 A:PHE318 4.5 30.0 1.0
HE1 A:PHE318 4.6 35.8 1.0
C A:PHE318 4.6 22.4 1.0
HG22 A:ILE223 4.6 31.9 1.0
CG1 A:ILE223 4.6 29.9 1.0
CB A:PHE318 4.7 25.0 1.0
CE1 A:PHE318 4.7 29.8 1.0
H031 A:E0Q504 4.7 32.4 1.0
C A:PRO317 4.8 21.2 1.0
CG A:PHE318 4.8 27.5 1.0
N A:PHE318 4.8 22.3 1.0
CD2 A:PHE237 4.9 20.1 1.0
CB A:ILE223 4.9 25.9 1.0
H112 A:E0Q504 5.0 34.6 1.0
HG2 A:PRO317 5.0 26.8 1.0
HD2 A:PHE237 5.0 24.1 1.0

Chlorine binding site 3 out of 4 in 6fp1

Go back to Chlorine Binding Sites List in 6fp1
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. 1


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. 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl502

b:22.7
occ:1.00
 H B:GLY322 2.3 18.9 1.0
HA B:PRO317 2.5 29.7 1.0
H B:GLN321 2.8 20.7 1.0
N B:GLY322 3.1 15.7 1.0
H1'2 B:FAD501 3.1 24.5 1.0
O B:HOH699 3.2 18.9 1.0
O B:HOH688 3.2 20.1 1.0
HA2 B:GLY320 3.2 25.3 1.0
C10 B:FAD501 3.3 19.6 1.0
HA3 B:GLY322 3.3 20.4 1.0
N10 B:FAD501 3.3 19.4 1.0
CA B:PRO317 3.4 24.7 1.0
N B:GLN321 3.4 17.2 1.0
HB3 B:PRO317 3.4 31.3 1.0
N1 B:FAD501 3.5 20.4 1.0
H B:GLY320 3.5 25.9 1.0
C1' B:FAD501 3.6 20.4 1.0
CB B:PRO317 3.7 26.1 1.0
CA B:GLY322 3.7 17.0 1.0
H1'1 B:FAD501 3.8 24.5 1.0
HB2 B:PRO317 3.8 31.3 1.0
CA B:GLY320 3.8 21.1 1.0
C4X B:FAD501 3.9 18.2 1.0
O B:PRO317 3.9 24.0 1.0
C9A B:FAD501 3.9 18.5 1.0
C B:GLY320 3.9 20.7 1.0
N B:GLY320 3.9 21.6 1.0
C B:PRO317 3.9 24.4 1.0
HG3 B:MET315 4.0 27.8 1.0
C B:GLN321 4.1 16.3 1.0
C2 B:FAD501 4.1 21.8 1.0
HA2 B:GLY322 4.3 20.4 1.0
O B:VAL316 4.3 22.4 1.0
CA B:GLN321 4.3 18.5 1.0
N5 B:FAD501 4.4 17.6 1.0
C5X B:FAD501 4.4 19.1 1.0
N B:PRO317 4.5 23.4 1.0
H B:MET323 4.5 18.8 0.5
H B:MET323 4.5 18.8 0.5
C4 B:FAD501 4.5 19.4 1.0
H B:HIS319 4.6 24.8 1.0
N3 B:FAD501 4.6 20.2 1.0
C9 B:FAD501 4.7 20.7 1.0
CG B:MET315 4.7 23.2 1.0
HG2 B:MET315 4.7 27.8 1.0
HA3 B:GLY320 4.7 25.3 1.0
C B:VAL316 4.7 22.5 1.0
O2 B:FAD501 4.8 20.5 1.0
SD B:MET315 4.9 23.7 1.0
HB2 B:GLN321 4.9 22.6 1.0
HA B:GLN321 4.9 22.2 1.0
C B:GLY322 5.0 16.3 1.0
O B:GLY320 5.0 20.4 1.0

Chlorine binding site 4 out of 4 in 6fp1

Go back to Chlorine Binding Sites List in 6fp1
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. 1


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. 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl507

b:29.5
occ:1.00
 CL9 B:E0Q507 0.0 29.5 1.0
C08 B:E0Q507 1.8 32.2 1.0
H073 B:E0Q507 2.5 45.3 1.0
C06 B:E0Q507 2.7 35.4 1.0
C02 B:E0Q507 2.7 31.1 1.0
HD13 B:ILE223 2.9 30.2 1.0
H011 B:E0Q507 2.9 37.3 1.0
C07 B:E0Q507 3.0 37.7 1.0
HA B:PHE318 3.0 28.9 1.0
HG21 B:ILE223 3.1 34.5 1.0
C01 B:E0Q507 3.1 31.1 1.0
H012 B:E0Q507 3.2 37.3 1.0
HD1 B:PHE318 3.3 34.7 1.0
H071 B:E0Q507 3.4 45.3 1.0
HE3 B:MET221 3.4 53.2 1.0
HE2 B:PHE237 3.5 28.8 1.0
HE1 B:MET221 3.5 53.2 1.0
H072 B:E0Q507 3.8 45.3 1.0
CD1 B:ILE223 3.8 25.2 1.0
CE B:MET221 3.9 44.4 1.0
CG2 B:ILE223 3.9 28.7 1.0
CA B:PHE318 4.0 24.1 1.0
CE2 B:PHE237 4.0 24.0 1.0
H013 B:E0Q507 4.0 37.3 1.0
C03 B:E0Q507 4.0 30.8 1.0
HG23 B:ILE223 4.0 34.5 1.0
O B:PRO317 4.0 24.0 1.0
HD12 B:ILE223 4.0 30.2 1.0
C05 B:E0Q507 4.1 35.5 1.0
CD1 B:PHE318 4.1 28.9 1.0
HD11 B:ILE223 4.2 30.2 1.0
HZ B:PHE237 4.3 28.5 1.0
O B:PHE318 4.3 23.8 1.0
HE2 B:MET221 4.4 53.2 1.0
C B:PHE318 4.4 23.9 1.0
CZ B:PHE237 4.4 23.8 1.0
HG22 B:ILE223 4.5 34.5 1.0
C04 B:E0Q507 4.5 33.5 1.0
HB3 B:PHE318 4.5 30.3 1.0
C B:PRO317 4.7 24.4 1.0
CB B:PHE318 4.7 25.3 1.0
H031 B:E0Q507 4.7 36.9 1.0
CG1 B:ILE223 4.7 26.5 1.0
N B:PHE318 4.8 23.6 1.0
HG12 B:ILE223 4.8 31.7 1.0
HE1 B:PHE318 4.8 36.3 1.0
CD2 B:PHE237 4.8 25.9 1.0
CB B:ILE223 4.9 26.7 1.0
HD2 B:PHE237 4.9 31.1 1.0
CG B:PHE318 4.9 27.6 1.0
CE1 B:PHE318 5.0 30.2 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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