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Chlorine in PDB 6n1k: Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State

Enzymatic activity of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State

All present enzymatic activity of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State:
1.14.16.1;

Protein crystallography data

The structure of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State, PDB code: 6n1k was solved by E.C.Arturo, E.K.Jaffe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.29 / 3.06
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 72.437, 202.640, 72.574, 90.00, 90.30, 90.00
R / Rfree (%) 20.3 / 23.8

Other elements in 6n1k:

The structure of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State (pdb code 6n1k). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State, PDB code: 6n1k:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 6n1k

Go back to Chlorine Binding Sites List in 6n1k
Chlorine binding site 1 out of 4 in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl501

b:0.7
occ:1.00
 HH21 A:ARG297 2.5 0.4 1.0
HH22 A:ARG297 2.6 0.4 1.0
NH2 A:ARG297 2.8 0.5 1.0
HE21 A:GLN301 3.3 0.7 1.0
HE2 B:TYR417 3.3 81.4 1.0
HH22 A:ARG261 3.3 90.2 1.0
HD2 B:TYR417 3.4 80.8 1.0
CE2 B:TYR417 3.8 67.8 1.0
CD2 B:TYR417 3.9 67.3 1.0
NE2 A:GLN301 4.0 93.1 1.0
NH2 A:ARG261 4.0 75.2 1.0
CZ A:ARG297 4.1 0.6 1.0
HE22 A:GLN301 4.2 0.7 1.0
HH12 A:ARG261 4.3 89.3 1.0
HH21 A:ARG261 4.3 90.2 1.0
HG2 A:GLN301 4.4 0.8 1.0
HE A:ARG297 4.6 0.1 1.0
HH12 A:ARG297 4.8 0.6 1.0
NE A:ARG297 4.8 0.9 1.0
CZ A:ARG261 4.8 74.5 1.0
NH1 A:ARG261 4.8 74.5 1.0
CZ B:TYR417 4.9 67.9 1.0
HH22 B:ARG413 4.9 0.9 1.0
NH1 A:ARG297 4.9 0.5 1.0
HH12 B:ARG413 4.9 0.7 1.0
CD A:GLN301 4.9 90.7 1.0
HH B:TYR417 5.0 82.3 1.0

Chlorine binding site 2 out of 4 in 6n1k

Go back to Chlorine Binding Sites List in 6n1k
Chlorine binding site 2 out of 4 in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl501

b:99.8
occ:1.00
 HH12 B:ARG297 2.0 95.8 1.0
HH22 B:ARG297 2.2 93.7 1.0
HH22 A:ARG71 2.4 0.8 1.0
NH1 B:ARG297 2.7 79.9 1.0
NH2 A:ARG71 2.8 0.2 1.0
NH2 B:ARG297 2.9 78.1 1.0
HH21 A:ARG71 2.9 0.8 1.0
HE21 B:GLN301 3.2 81.4 1.0
CZ B:ARG297 3.2 79.3 1.0
HH22 B:ARG261 3.4 87.4 1.0
HH11 B:ARG297 3.4 95.8 1.0
HE2 A:TYR417 3.5 86.5 1.0
HH21 B:ARG297 3.6 93.7 1.0
CZ A:ARG71 3.8 0.8 1.0
HD2 A:TYR417 3.9 85.8 1.0
NE2 B:GLN301 3.9 67.8 1.0
HH12 A:ARG71 4.0 0.7 1.0
CE2 A:TYR417 4.1 72.1 1.0
HE22 B:GLN301 4.1 81.4 1.0
NH2 B:ARG261 4.1 72.8 1.0
HG2 B:GLN301 4.3 80.2 1.0
NH1 A:ARG71 4.3 99.7 1.0
CD2 A:TYR417 4.3 71.5 1.0
HH21 B:ARG261 4.4 87.4 1.0
NE B:ARG297 4.5 82.1 1.0
HH12 B:ARG261 4.6 86.4 1.0
NE A:ARG71 4.8 98.9 1.0
HE A:ARG71 4.8 0.7 1.0
CD B:GLN301 4.8 67.8 1.0
CG B:GLN301 5.0 66.8 1.0
HE B:ARG297 5.0 98.6 1.0

Chlorine binding site 3 out of 4 in 6n1k

Go back to Chlorine Binding Sites List in 6n1k
Chlorine binding site 3 out of 4 in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl501

b:99.4
occ:1.00
 HH21 C:ARG297 2.4 0.7 1.0
NH2 C:ARG297 2.5 96.4 1.0
HH22 C:ARG297 2.5 0.7 1.0
HH22 C:ARG261 2.7 99.2 1.0
HE21 C:GLN301 2.8 0.6 1.0
CZ C:ARG297 3.2 97.8 1.0
HE2 D:TYR417 3.2 93.4 1.0
NH2 C:ARG261 3.4 82.7 1.0
NE2 C:GLN301 3.5 88.0 1.0
HD2 D:TYR417 3.6 92.8 1.0
HG2 C:GLN301 3.6 0.1 1.0
HH21 C:ARG261 3.7 99.2 1.0
CE2 D:TYR417 3.7 77.9 1.0
HE C:ARG297 3.7 0.2 1.0
NE C:ARG297 3.8 98.5 1.0
HE22 C:GLN301 3.9 0.6 1.0
NH1 C:ARG297 3.9 98.1 1.0
HH12 C:ARG297 3.9 0.7 1.0
CD2 D:TYR417 3.9 77.3 1.0
HH12 C:ARG261 4.0 98.1 1.0
CZ C:ARG261 4.3 81.8 1.0
CD C:GLN301 4.3 87.7 1.0
CG C:GLN301 4.3 85.1 1.0
NH1 C:ARG261 4.5 81.7 1.0
HH11 C:ARG297 4.5 0.7 1.0
HG3 C:GLN301 4.6 0.1 1.0
HH D:TYR417 4.7 94.3 1.0
HG3 C:ARG297 4.7 0.8 1.0
CZ D:TYR417 4.7 77.9 1.0
HG2 C:ARG297 4.8 0.8 1.0
CD C:ARG297 5.0 96.7 1.0

Chlorine binding site 4 out of 4 in 6n1k

Go back to Chlorine Binding Sites List in 6n1k
Chlorine binding site 4 out of 4 in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl501

b:99.5
occ:1.00
 HH11 D:ARG297 2.4 98.9 1.0
HH12 D:ARG297 2.6 98.9 1.0
NH1 D:ARG297 2.8 82.4 1.0
HE21 D:GLN301 3.0 90.0 1.0
HH22 D:ARG261 3.0 0.9 1.0
HH22 C:ARG71 3.3 0.8 1.0
HE2 C:TYR417 3.4 90.5 1.0
NE2 D:GLN301 3.6 75.0 1.0
HD2 C:TYR417 3.6 89.8 1.0
NH2 D:ARG261 3.8 91.6 1.0
HD3 D:ARG297 3.9 0.9 1.0
HE22 D:GLN301 3.9 90.0 1.0
CE2 C:TYR417 3.9 75.4 1.0
NH2 C:ARG71 4.0 0.1 1.0
CZ D:ARG297 4.1 82.5 1.0
CD2 C:TYR417 4.1 74.8 1.0
HH21 D:ARG261 4.1 0.9 1.0
HG2 D:GLN301 4.1 88.5 1.0
HH12 C:ARG71 4.2 0.7 1.0
HH12 D:ARG261 4.2 0.5 1.0
HH21 C:ARG71 4.4 0.8 1.0
CD D:GLN301 4.6 75.0 1.0
CD D:ARG297 4.7 84.1 1.0
NH1 C:ARG71 4.7 0.6 1.0
CZ D:ARG261 4.7 90.5 1.0
CZ C:ARG71 4.8 0.6 1.0
NH1 D:ARG261 4.8 90.4 1.0
CG D:GLN301 4.8 73.8 1.0
HH22 D:ARG297 4.8 98.5 1.0
NE D:ARG297 4.8 83.3 1.0
HH22 C:ARG413 4.8 0.6 1.0
NH2 D:ARG297 4.9 82.1 1.0
HG2 D:ARG297 4.9 0.3 1.0
HG3 D:ARG297 4.9 0.3 1.0
HG3 D:GLN301 5.0 88.5 1.0
HH C:TYR417 5.0 92.0 1.0

Reference:

E.C.Arturo, K.Gupta, M.R.Hansen, E.Borne, E.K.Jaffe. Biophysical Characterization of Full-Length Human Phenylalanine Hydroxylase Provides A Deeper Understanding of Its Quaternary Structure Equilibrium. J.Biol.Chem. V. 294 10131 2019.
ISSN: ESSN 1083-351X
PubMed: 31076506
DOI: 10.1074/JBC.RA119.008294
Page generated: Sun Jul 28 03:29:22 2024

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