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Iron in PDB 1mmt: Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) Complexed with Tetrahydrobiopterin and Norleucine

Enzymatic activity of Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) Complexed with Tetrahydrobiopterin and Norleucine

All present enzymatic activity of Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) Complexed with Tetrahydrobiopterin and Norleucine:
1.14.16.1;

Protein crystallography data

The structure of Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) Complexed with Tetrahydrobiopterin and Norleucine, PDB code: 1mmt was solved by O.A.Andersen, T.Flatmark, E.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 65.140, 106.638, 123.611, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 24.3

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) Complexed with Tetrahydrobiopterin and Norleucine (pdb code 1mmt). 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 Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) Complexed with Tetrahydrobiopterin and Norleucine, PDB code: 1mmt:

Iron binding site 1 out of 1 in 1mmt

Go back to Iron Binding Sites List in 1mmt
Iron binding site 1 out of 1 in the Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) Complexed with Tetrahydrobiopterin and Norleucine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) Complexed with Tetrahydrobiopterin and Norleucine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1425

b:32.1
occ:1.00
 O A:HOH575 2.1 51.8 1.0
NE2 A:HIS285 2.1 17.1 1.0
NE2 A:HIS290 2.3 21.1 1.0
OE2 A:GLU330 2.3 25.2 1.0
OE1 A:GLU330 2.4 22.0 1.0
CD A:GLU330 2.7 22.8 1.0
CE1 A:HIS285 3.0 15.0 1.0
CD2 A:HIS290 3.1 21.0 1.0
CD2 A:HIS285 3.2 14.9 1.0
CE1 A:HIS290 3.3 22.4 1.0
O4 A:H4B1426 3.5 27.5 1.0
N5 A:H4B1426 3.8 24.3 1.0
CE A:NLE1427 4.1 20.5 1.0
ND1 A:HIS285 4.2 19.0 1.0
CG A:GLU330 4.2 23.0 1.0
CG A:HIS285 4.3 17.3 1.0
CG A:HIS290 4.3 20.6 1.0
C4 A:H4B1426 4.4 26.3 1.0
O9 A:H4B1426 4.4 23.9 1.0
ND1 A:HIS290 4.4 21.3 1.0
C4A A:H4B1426 4.6 24.7 1.0
CD A:NLE1427 4.7 19.5 1.0
CB A:ALA345 4.7 17.9 1.0
C9 A:H4B1426 4.8 25.3 1.0
OE2 A:GLU286 4.8 18.8 1.0

Reference:

O.A.Andersen, A.J.Stokka, T.Flatmark, E.Hough. 2.0A Resolution Crystal Structures of the Ternary Complexes of Human Phenylalanine Hydroxylase Catalytic Domain with Tetrahydrobiopterin and 3-(2-Thienyl)-L-Alanine or L-Norleucine: Substrate Specificity and Molecular Motions Related to Substrate Binding J.Mol.Biol. V. 333 747 2003.
ISSN: ISSN 0022-2836
PubMed: 14568534
DOI: 10.1016/J.JMB.2003.09.004
Page generated: Sun Dec 13 14:24:08 2020

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