Iron in PDB 6pah: Human Phenylalanine Hydroxylase Catalytic Domain Dimer with Bound L- Dopa (3,4-Dihydroxyphenylalanine) Inhibitor

Enzymatic activity of Human Phenylalanine Hydroxylase Catalytic Domain Dimer with Bound L- Dopa (3,4-Dihydroxyphenylalanine) Inhibitor

All present enzymatic activity of Human Phenylalanine Hydroxylase Catalytic Domain Dimer with Bound L- Dopa (3,4-Dihydroxyphenylalanine) Inhibitor:
1.14.16.1;

Protein crystallography data

The structure of Human Phenylalanine Hydroxylase Catalytic Domain Dimer with Bound L- Dopa (3,4-Dihydroxyphenylalanine) Inhibitor, PDB code: 6pah was solved by H.Erlandsen, T.Flatmark, R.C.Stevens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.15
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 66.890, 109.120, 125.710, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 20.3

Iron Binding Sites:

The binding sites of Iron atom in the Human Phenylalanine Hydroxylase Catalytic Domain Dimer with Bound L- Dopa (3,4-Dihydroxyphenylalanine) Inhibitor (pdb code 6pah). 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 Human Phenylalanine Hydroxylase Catalytic Domain Dimer with Bound L- Dopa (3,4-Dihydroxyphenylalanine) Inhibitor, PDB code: 6pah:

Iron binding site 1 out of 1 in 6pah

Go back to Iron Binding Sites List in 6pah
Iron binding site 1 out of 1 in the Human Phenylalanine Hydroxylase Catalytic Domain Dimer with Bound L- Dopa (3,4-Dihydroxyphenylalanine) Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Phenylalanine Hydroxylase Catalytic Domain Dimer with Bound L- Dopa (3,4-Dihydroxyphenylalanine) Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe425

b:21.9
occ:1.00
 OZ A:DAH600 2.1 52.9 1.0
OE2 A:DAH600 2.1 52.3 1.0
OE2 A:GLU330 2.2 21.9 1.0
NE2 A:HIS290 2.2 14.9 1.0
NE2 A:HIS285 2.2 17.1 1.0
O A:HOH649 2.4 13.9 1.0
CZ A:DAH600 2.7 53.4 1.0
CE2 A:DAH600 2.7 53.4 1.0
CD A:GLU330 3.1 20.9 1.0
CE1 A:HIS290 3.1 14.0 1.0
CD2 A:HIS290 3.2 14.4 1.0
CE1 A:HIS285 3.2 17.6 1.0
CD2 A:HIS285 3.2 17.0 1.0
OE1 A:GLU330 3.4 21.9 1.0
CE1 A:DAH600 4.1 53.7 1.0
CD2 A:DAH600 4.1 53.9 1.0
ND1 A:HIS290 4.2 15.1 1.0
CG A:GLU330 4.3 19.4 1.0
OE1 A:GLU286 4.3 17.9 1.0
CG A:HIS290 4.3 15.2 1.0
ND1 A:HIS285 4.3 17.5 1.0
CG A:HIS285 4.4 17.5 1.0
OH A:TYR325 4.5 19.2 1.0
CB A:ALA345 4.6 14.5 1.0
O A:HOH621 4.8 45.8 1.0
CB A:PRO281 4.8 17.9 1.0

Reference:

H.Erlandsen, T.Flatmark, R.C.Stevens, E.Hough. Crystallographic Analysis of the Human Phenylalanine Hydroxylase Catalytic Domain with Bound Catechol Inhibitors at 2.0 A Resolution. Biochemistry V. 37 15638 1998.
ISSN: ISSN 0006-2960
PubMed: 9843368
DOI: 10.1021/BI9815290
Page generated: Sun Dec 13 16:48:32 2020

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