Atomistry » Iron » PDB 4a9v-4b2y » 4anp
Atomistry »
  Iron »
    PDB 4a9v-4b2y »
      4anp »

Iron in PDB 4anp: Crystal Structure of Human Phenylalanine Hydroxylase in Complex with A Pharmacological Chaperone

Enzymatic activity of Crystal Structure of Human Phenylalanine Hydroxylase in Complex with A Pharmacological Chaperone

All present enzymatic activity of Crystal Structure of Human Phenylalanine Hydroxylase in Complex with A Pharmacological Chaperone:
1.14.16.1;

Protein crystallography data

The structure of Crystal Structure of Human Phenylalanine Hydroxylase in Complex with A Pharmacological Chaperone, PDB code: 4anp was solved by R.Torreblanca, E.Lira-Navarrete, J.Sancho, R.Hurtado-Guerrero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 62.28 / 2.11
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 66.283, 107.511, 124.550, 90.00, 90.00, 90.00
R / Rfree (%) 20.381 / 23.652

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Human Phenylalanine Hydroxylase in Complex with A Pharmacological Chaperone (pdb code 4anp). 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 Human Phenylalanine Hydroxylase in Complex with A Pharmacological Chaperone, PDB code: 4anp:

Iron binding site 1 out of 1 in 4anp

Go back to Iron Binding Sites List in 4anp
Iron binding site 1 out of 1 in the Crystal Structure of Human Phenylalanine Hydroxylase in Complex with A Pharmacological Chaperone


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 Human Phenylalanine Hydroxylase in Complex with A Pharmacological Chaperone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1426

b:17.9
occ:1.00
 OE2 A:GLU330 2.0 19.6 1.0
NE2 A:HIS290 2.1 13.7 1.0
NAJ A:3QI1427 2.1 29.2 1.0
NE2 A:HIS285 2.1 17.2 1.0
O A:HOH2136 2.3 24.0 1.0
CD A:GLU330 2.8 18.6 1.0
CAP A:3QI1427 2.9 30.5 1.0
CE1 A:HIS290 3.0 13.7 1.0
SAE A:3QI1427 3.0 30.2 1.0
OE1 A:GLU330 3.0 20.5 1.0
CE1 A:HIS285 3.0 17.3 1.0
CD2 A:HIS290 3.1 13.4 1.0
CD2 A:HIS285 3.2 17.1 1.0
CAR A:3QI1427 3.2 31.2 1.0
SAK A:3QI1427 3.9 29.5 1.0
ND1 A:HIS290 4.1 14.0 1.0
CG A:GLU330 4.2 17.9 1.0
ND1 A:HIS285 4.2 17.6 1.0
NAT A:3QI1427 4.2 31.6 1.0
CG A:HIS290 4.2 14.1 1.0
OE1 A:GLU286 4.3 18.4 1.0
CG A:HIS285 4.3 17.9 1.0
OH A:TYR325 4.4 15.9 1.0
CB A:ALA345 4.5 13.9 1.0
CAS A:3QI1427 4.5 30.2 1.0
O A:HOH2152 4.8 29.2 1.0
O A:HOH2125 4.9 29.4 1.0
CAQ A:3QI1427 4.9 31.8 1.0

Reference:

R.Torreblanca, E.Lira-Navarrete, J.Sancho, R.Hurtado-Guerrero. Structural and Mechanistic Basis of the Interaction Between A Pharmacological Chaperone and Human Phenylalanine Hydroxylase. Chembiochem V. 13 1266 2012.
ISSN: ISSN 1439-4227
PubMed: 22549968
DOI: 10.1002/CBIC.201200188
Page generated: Sun Aug 4 23:41:26 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy