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Iron in PDB 1tg2: Crystal Structure of Phenylalanine Hydroxylase A313T Mutant with 7,8-Dihydrobiopterin Bound

Enzymatic activity of Crystal Structure of Phenylalanine Hydroxylase A313T Mutant with 7,8-Dihydrobiopterin Bound

All present enzymatic activity of Crystal Structure of Phenylalanine Hydroxylase A313T Mutant with 7,8-Dihydrobiopterin Bound:
1.14.16.1;

Protein crystallography data

The structure of Crystal Structure of Phenylalanine Hydroxylase A313T Mutant with 7,8-Dihydrobiopterin Bound, PDB code: 1tg2 was solved by H.Erlandsen, A.L.Pey, A.Gamez, B.Perez, L.R.Desviat, C.Aguado, R.Koch, S.Surendran, S.Tyring, R.Matalon, C.R.Scriver, M.Ugarte, A.Martinez, R.C.Stevens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.91 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 66.534, 107.755, 124.282, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 25.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Phenylalanine Hydroxylase A313T Mutant with 7,8-Dihydrobiopterin Bound (pdb code 1tg2). 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 Phenylalanine Hydroxylase A313T Mutant with 7,8-Dihydrobiopterin Bound, PDB code: 1tg2:

Iron binding site 1 out of 1 in 1tg2

Go back to Iron Binding Sites List in 1tg2
Iron binding site 1 out of 1 in the Crystal Structure of Phenylalanine Hydroxylase A313T Mutant with 7,8-Dihydrobiopterin Bound


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 Phenylalanine Hydroxylase A313T Mutant with 7,8-Dihydrobiopterin Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe425

b:38.4
occ:1.00
 OE2 A:GLU330 1.9 41.0 1.0
NE2 A:HIS290 2.1 31.8 1.0
NE2 A:HIS285 2.1 18.2 1.0
O A:HOH484 2.5 34.0 1.0
O A:HOH442 2.6 42.4 1.0
CD A:GLU330 2.9 41.7 1.0
CE1 A:HIS290 3.0 27.2 1.0
CE1 A:HIS285 3.0 18.5 1.0
OE1 A:GLU330 3.1 47.5 1.0
CD2 A:HIS290 3.2 30.0 1.0
CD2 A:HIS285 3.2 16.7 1.0
O4 A:H2B426 3.9 38.8 1.0
ND1 A:HIS290 4.1 31.0 1.0
ND1 A:HIS285 4.2 21.7 1.0
CG A:GLU330 4.2 38.7 1.0
CG A:HIS290 4.3 30.1 1.0
CG A:HIS285 4.3 19.5 1.0
OE1 A:GLU286 4.4 23.9 1.0
CB A:ALA345 4.6 20.1 1.0
OH A:TYR325 4.7 32.6 1.0
CB A:PRO281 4.8 40.9 1.0

Reference:

H.Erlandsen, A.L.Pey, A.Gamez, B.Perez, L.R.Desviat, C.Aguado, R.Koch, S.Surendran, S.Tyring, R.Matalon, C.R.Scriver, M.Ugarte, A.Martinez, R.C.Stevens. Correction of Kinetic and Stability Defects By Tetrahydrobiopterin in Phenylketonuria Patients with Certain Phenylalanine Hydroxylase Mutations. Proc.Natl.Acad.Sci.Usa V. 101 16903 2004.
ISSN: ISSN 0027-8424
PubMed: 15557004
DOI: 10.1073/PNAS.0407256101
Page generated: Sat Aug 3 15:16:15 2024

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