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Iron 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:

Chlorine (Cl) 4 atoms

Iron Binding Sites:

The binding sites of Iron 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 Iron atom.
In total 4 binding sites of Iron where determined in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State, PDB code: 6n1k:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 6n1k

Go back to Iron Binding Sites List in 6n1k
Iron 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 Iron with other atoms in the Fe 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:Fe502

b:1.0
occ:1.00
NE2 A:HIS290 2.2 95.3 1.0
O A:HOH602 2.2 0.9 1.0
NE2 A:HIS285 2.2 0.3 1.0
O A:HOH601 2.2 0.6 1.0
OE2 A:GLU330 2.2 70.6 1.0
CE1 A:HIS290 2.9 91.7 1.0
HE1 A:HIS290 3.0 0.0 1.0
CD A:GLU330 3.0 71.2 1.0
CE1 A:HIS285 3.1 0.7 1.0
OE1 A:GLU330 3.1 71.8 1.0
HE1 A:HIS285 3.2 0.7 1.0
CD2 A:HIS290 3.2 0.0 1.0
CD2 A:HIS285 3.2 0.4 1.0
HD2 A:HIS285 3.5 0.9 1.0
HD2 A:HIS290 3.5 0.8 1.0
HH A:TYR325 3.7 75.6 1.0
OE1 A:GLU286 3.8 70.0 1.0
ND1 A:HIS290 4.0 0.1 1.0
HB3 A:ALA345 4.1 0.1 1.0
CG A:HIS290 4.2 73.8 1.0
ND1 A:HIS285 4.2 0.1 1.0
HB3 A:PRO281 4.3 0.1 1.0
CG A:HIS285 4.4 97.9 1.0
HE2 A:TYR325 4.4 77.6 1.0
HB1 A:ALA345 4.4 0.1 1.0
CG A:GLU330 4.5 71.5 1.0
OH A:TYR325 4.5 63.0 1.0
HZ A:PHE263 4.6 96.5 1.0
CD A:GLU286 4.7 70.5 1.0
CB A:ALA345 4.7 85.1 1.0
HG2 A:GLU330 4.7 85.8 1.0
HD1 A:HIS290 4.7 0.9 1.0
HE1 A:PHE263 4.7 96.5 1.0
HG3 A:GLU330 4.8 85.8 1.0
OE2 A:GLU286 4.8 70.6 1.0

Iron binding site 2 out of 4 in 6n1k

Go back to Iron Binding Sites List in 6n1k
Iron 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 Iron with other atoms in the Fe 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:Fe502

b:0.7
occ:1.00
NE2 B:HIS285 2.1 0.9 1.0
O B:HOH602 2.2 0.4 1.0
NE2 B:HIS290 2.2 80.6 1.0
O B:HOH601 2.2 0.1 1.0
OE1 B:GLU330 2.2 87.4 1.0
CE1 B:HIS290 3.0 79.2 1.0
CD B:GLU330 3.0 88.0 1.0
CD2 B:HIS285 3.1 0.8 1.0
HE1 B:HIS290 3.1 95.1 1.0
OE2 B:GLU330 3.1 88.3 1.0
CE1 B:HIS285 3.2 0.1 1.0
CD2 B:HIS290 3.2 79.4 1.0
HD2 B:HIS285 3.2 0.4 1.0
HE1 B:HIS285 3.4 0.1 1.0
HD2 B:HIS290 3.4 95.3 1.0
OH B:TYR325 4.1 71.3 1.0
ND1 B:HIS290 4.1 78.2 1.0
HG2 B:GLU286 4.1 0.9 1.0
HB3 B:PRO281 4.2 86.8 1.0
CG B:HIS290 4.2 78.5 1.0
CG B:HIS285 4.2 0.1 1.0
ND1 B:HIS285 4.3 1.0 1.0
HB3 B:ALA345 4.3 93.5 1.0
CG B:GLU330 4.5 88.7 1.0
HE2 B:TYR325 4.5 87.7 1.0
HH B:TYR325 4.5 85.5 1.0
HZ B:PHE263 4.5 93.0 1.0
HE1 B:PHE263 4.6 92.1 1.0
HG2 B:GLU330 4.7 0.4 1.0
HG3 B:GLU330 4.8 0.4 1.0
HB1 B:ALA345 4.8 93.5 1.0
HD1 B:HIS290 4.8 93.9 1.0
CG B:GLU286 5.0 94.1 1.0

Iron binding site 3 out of 4 in 6n1k

Go back to Iron Binding Sites List in 6n1k
Iron 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 Iron with other atoms in the Fe 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:Fe502

b:0.4
occ:1.00
OE2 C:GLU330 2.1 0.1 1.0
NE2 C:HIS285 2.1 0.1 1.0
NE2 C:HIS290 2.2 67.1 1.0
O C:HOH601 2.2 0.4 1.0
OE1 C:GLU330 2.3 0.6 1.0
CD C:GLU330 2.5 0.8 1.0
CE1 C:HIS290 2.9 66.5 1.0
HE1 C:HIS290 2.9 79.8 1.0
CE1 C:HIS285 3.0 96.9 1.0
HE1 C:HIS285 3.1 0.3 1.0
CD2 C:HIS285 3.3 0.5 1.0
CD2 C:HIS290 3.4 66.9 1.0
HD2 C:HIS285 3.5 0.4 1.0
HH C:TYR325 3.6 82.2 1.0
HD2 C:HIS290 3.7 80.3 1.0
HB3 C:ALA345 3.9 96.1 1.0
CG C:GLU330 4.0 72.3 1.0
ND1 C:HIS290 4.1 65.9 1.0
ND1 C:HIS285 4.2 0.4 1.0
OH C:TYR325 4.3 68.5 1.0
CG C:HIS285 4.3 79.6 1.0
CG C:HIS290 4.4 66.1 1.0
HB1 C:ALA345 4.4 96.1 1.0
HB3 C:PRO281 4.5 0.7 1.0
HE2 C:TYR325 4.5 83.9 1.0
CB C:ALA345 4.6 80.0 1.0
HG2 C:GLU286 4.7 97.9 1.0
HZ C:PHE263 4.7 0.8 1.0
HG3 C:PRO281 4.7 0.8 1.0
HD1 C:HIS290 4.8 79.0 1.0
HD1 C:HIS285 4.9 0.2 1.0
CB C:GLU330 4.9 66.8 1.0
HB2 C:ALA345 5.0 96.1 1.0
HE1 C:PHE263 5.0 0.7 1.0

Iron binding site 4 out of 4 in 6n1k

Go back to Iron Binding Sites List in 6n1k
Iron 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 Iron with other atoms in the Fe 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:Fe502

b:0.5
occ:1.00
NE2 D:HIS285 2.2 75.8 1.0
OE2 D:GLU330 2.2 98.4 1.0
O D:HOH602 2.2 0.2 1.0
NE2 D:HIS290 2.2 72.0 1.0
O D:HOH601 2.2 99.8 1.0
CE1 D:HIS290 2.9 71.6 1.0
CD D:GLU330 3.0 99.4 1.0
CE1 D:HIS285 3.0 73.5 1.0
OE1 D:GLU330 3.2 100.0 1.0
CD2 D:HIS285 3.2 88.6 1.0
CD2 D:HIS290 3.2 71.7 1.0
HH D:TYR325 3.5 0.4 1.0
OE2 D:GLU286 3.9 82.3 1.0
ND1 D:HIS290 4.0 71.0 1.0
HB3 D:PRO281 4.2 0.8 1.0
CG D:HIS290 4.2 71.0 1.0
ND1 D:HIS285 4.2 89.1 1.0
CG D:HIS285 4.3 73.5 1.0
OH D:TYR325 4.3 0.2 1.0
HB3 D:ALA345 4.4 0.8 1.0
HE2 D:TYR325 4.4 0.3 1.0
CG D:GLU330 4.5 0.0 1.0
HZ D:PHE263 4.6 81.7 1.0
HG2 D:GLU330 4.7 0.0 1.0
CD D:GLU286 4.7 79.5 1.0
HE1 D:PHE263 4.7 81.4 1.0
HG3 D:GLU330 4.7 0.0 1.0
HB1 D:ALA345 4.8 0.8 1.0
OE1 D:GLU286 4.9 80.8 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: Wed Aug 7 02:39:27 2024

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