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Iron in PDB 5den: The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer

Enzymatic activity of The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer

All present enzymatic activity of The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer:
1.14.16.1;

Protein crystallography data

The structure of The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer, PDB code: 5den was solved by E.C.Arturo, P.J.Loll, E.K.Jaffe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.10 / 2.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 113.780, 89.160, 196.810, 90.00, 104.53, 90.00
R / Rfree (%) 23.8 / 30.3

Iron Binding Sites:

The binding sites of Iron atom in the The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer (pdb code 5den). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer, PDB code: 5den:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 5den

Go back to Iron Binding Sites List in 5den
Iron binding site 1 out of 4 in the The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:59.1
occ:0.80
 OE2 A:GLU330 2.1 80.4 1.0
NE2 A:HIS285 2.2 81.0 1.0
NE2 A:HIS290 2.2 79.4 1.0
O A:HOH601 2.3 31.7 1.0
O A:HOH602 2.3 72.1 1.0
CE1 A:HIS290 2.8 78.7 1.0
CD A:GLU330 2.9 72.5 1.0
OE1 A:GLU330 3.1 86.8 1.0
CD2 A:HIS285 3.1 81.4 1.0
CE1 A:HIS285 3.2 73.8 1.0
CD2 A:HIS290 3.4 89.1 1.0
ND1 A:HIS290 4.0 83.6 1.0
OH A:TYR325 4.1 80.0 1.0
ND1 A:HIS285 4.3 51.0 1.0
CG A:HIS285 4.3 72.7 1.0
CG A:GLU330 4.3 75.9 1.0
CG A:HIS290 4.3 85.5 1.0
OE1 A:GLU286 4.5 72.5 1.0
CB A:ALA345 4.8 68.6 1.0
CG A:PRO281 5.0 68.6 1.0

Iron binding site 2 out of 4 in 5den

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Iron binding site 2 out of 4 in the The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:44.8
occ:0.55
 OE2 B:GLU330 2.1 88.2 1.0
NE2 B:HIS290 2.2 0.9 1.0
NE2 B:HIS285 2.2 95.2 1.0
O B:HOH601 2.3 32.5 1.0
O B:HOH602 2.3 62.7 1.0
CE1 B:HIS290 2.8 98.2 1.0
CD B:GLU330 2.8 80.9 1.0
OE1 B:GLU330 2.9 79.2 1.0
CD2 B:HIS285 3.1 93.6 1.0
CE1 B:HIS285 3.2 93.9 1.0
CD2 B:HIS290 3.4 95.4 1.0
OH B:TYR325 3.7 95.0 1.0
ND1 B:HIS290 4.0 84.1 1.0
CG B:GLU330 4.3 73.7 1.0
ND1 B:HIS285 4.3 79.4 1.0
CG B:HIS285 4.3 84.7 1.0
CG B:HIS290 4.3 72.6 1.0
OE1 B:GLU286 4.5 0.7 1.0
CB B:ALA345 4.6 59.4 1.0
CZ B:TYR325 4.7 89.5 1.0
CE2 B:TYR325 4.9 91.8 1.0
CG B:PRO281 4.9 90.6 1.0

Iron binding site 3 out of 4 in 5den

Go back to Iron Binding Sites List in 5den
Iron binding site 3 out of 4 in the The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:49.1
occ:0.61
 OE2 C:GLU330 2.1 99.6 1.0
NE2 C:HIS290 2.2 82.7 1.0
NE2 C:HIS285 2.3 0.2 1.0
O C:HOH601 2.3 56.0 1.0
O C:HOH602 2.4 48.5 1.0
CE1 C:HIS290 2.8 86.5 1.0
CD C:GLU330 2.8 0.6 1.0
OE1 C:GLU330 3.0 0.8 1.0
CD2 C:HIS285 3.2 0.6 1.0
CE1 C:HIS285 3.3 94.4 1.0
CD2 C:HIS290 3.3 83.5 1.0
OH C:TYR325 3.9 99.3 1.0
ND1 C:HIS290 4.0 80.2 1.0
CG C:HIS290 4.3 73.3 1.0
CG C:GLU330 4.3 94.0 1.0
CG C:HIS285 4.4 92.9 1.0
ND1 C:HIS285 4.4 86.8 1.0
OE1 C:GLU286 4.5 86.8 1.0
CB C:ALA345 4.7 86.0 1.0
CZ C:TYR325 4.9 81.5 1.0

Iron binding site 4 out of 4 in 5den

Go back to Iron Binding Sites List in 5den
Iron binding site 4 out of 4 in the The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The First Structure of A Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Auto-Inhibited Tetramer within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:83.2
occ:0.86
 OE2 D:GLU330 2.1 91.7 1.0
NE2 D:HIS290 2.2 84.8 1.0
NE2 D:HIS285 2.2 82.6 1.0
O D:HOH602 2.3 54.4 1.0
O D:HOH601 2.3 87.3 1.0
CE1 D:HIS290 3.0 81.0 1.0
CD D:GLU330 3.0 84.8 1.0
CD2 D:HIS285 3.1 79.2 1.0
OE1 D:GLU330 3.2 87.6 1.0
CD2 D:HIS290 3.3 80.3 1.0
CE1 D:HIS285 3.3 79.2 1.0
ND1 D:HIS290 4.1 72.8 1.0
OE1 D:GLU286 4.3 67.3 1.0
CG D:HIS285 4.3 68.6 1.0
CG D:HIS290 4.3 64.7 1.0
ND1 D:HIS285 4.3 53.8 1.0
OH D:TYR325 4.4 70.7 1.0
CG D:GLU330 4.4 84.0 1.0
CB D:ALA345 4.6 75.7 1.0
CG D:PRO281 4.6 71.5 1.0
CB D:PRO281 4.7 61.4 1.0

Reference:

E.C.Arturo, K.Gupta, A.Heroux, L.Stith, P.J.Cross, E.J.Parker, P.J.Loll, E.K.Jaffe. First Structure of Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture of An Autoinhibited Tetramer. Proc.Natl.Acad.Sci.Usa V. 113 2394 2016.
ISSN: ESSN 1091-6490
PubMed: 26884182
DOI: 10.1073/PNAS.1516967113
Page generated: Tue Aug 5 20:44:27 2025

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