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Iron in PDB 6hpo: Crystallographic Structure of the Catalytic Domain of Human Phenylalanine Hydroxylase (Hpah Cd) in Complex with Iron at 1.6 Angstrom

Enzymatic activity of Crystallographic Structure of the Catalytic Domain of Human Phenylalanine Hydroxylase (Hpah Cd) in Complex with Iron at 1.6 Angstrom

All present enzymatic activity of Crystallographic Structure of the Catalytic Domain of Human Phenylalanine Hydroxylase (Hpah Cd) in Complex with Iron at 1.6 Angstrom:
1.14.16.1;

Protein crystallography data

The structure of Crystallographic Structure of the Catalytic Domain of Human Phenylalanine Hydroxylase (Hpah Cd) in Complex with Iron at 1.6 Angstrom, PDB code: 6hpo was solved by M.Alcorlo Pages, M.Innselset Flydal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.77 / 1.67
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 65.856, 107.549, 124.016, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 17.7

Iron Binding Sites:

The binding sites of Iron atom in the Crystallographic Structure of the Catalytic Domain of Human Phenylalanine Hydroxylase (Hpah Cd) in Complex with Iron at 1.6 Angstrom (pdb code 6hpo). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystallographic Structure of the Catalytic Domain of Human Phenylalanine Hydroxylase (Hpah Cd) in Complex with Iron at 1.6 Angstrom, PDB code: 6hpo:

Iron binding site 1 out of 1 in 6hpo

Go back to Iron Binding Sites List in 6hpo
Iron binding site 1 out of 1 in the Crystallographic Structure of the Catalytic Domain of Human Phenylalanine Hydroxylase (Hpah Cd) in Complex with Iron at 1.6 Angstrom


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystallographic Structure of the Catalytic Domain of Human Phenylalanine Hydroxylase (Hpah Cd) in Complex with Iron at 1.6 Angstrom within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:27.1
occ:1.00
 NE2 A:HIS285 2.1 26.1 1.0
NE2 A:HIS290 2.1 22.8 1.0
OE2 A:GLU330 2.2 48.4 1.0
O A:HOH809 2.3 30.9 1.0
O A:HOH608 2.3 39.3 1.0
O A:HOH618 2.3 31.3 1.0
OE1 A:GLU330 2.7 43.5 1.0
CD A:GLU330 2.8 36.6 1.0
CE1 A:HIS285 3.1 25.8 1.0
CD2 A:HIS290 3.1 23.0 1.0
CD2 A:HIS285 3.1 24.2 1.0
CE1 A:HIS290 3.1 24.8 1.0
O A:HOH846 3.8 64.4 1.0
ND1 A:HIS285 4.2 26.7 1.0
ND1 A:HIS290 4.2 22.0 1.0
CG A:HIS290 4.2 22.6 1.0
CG A:GLU330 4.2 32.5 1.0
CG A:HIS285 4.2 25.1 1.0
O A:HOH840 4.3 37.4 1.0
OH A:TYR325 4.3 31.8 1.0
OE1 A:GLU286 4.3 31.3 1.0
CB A:ALA345 4.6 21.6 1.0
O A:HOH822 4.8 42.8 1.0
O A:HOH673 4.9 51.3 1.0

Reference:

M.I.Flydal, M.Alcorlo-Pages, F.G.Johannessen, S.Martinez-Caballero, L.SkjæRven, R.Fernandez-Leiro, A.Martinez, J.A.Hermoso. Structure of Full-Length Human Phenylalanine Hydroxylase in Complex with Tetrahydrobiopterin. Proc.Natl.Acad.Sci.Usa V. 116 11229 2019.
ISSN: ESSN 1091-6490
PubMed: 31118288
DOI: 10.1073/PNAS.1902639116
Page generated: Tue Aug 6 21:33:02 2024

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