Atomistry » Iron » PDB 2rfc-2v1i » 2toh
Atomistry »
  Iron »
    PDB 2rfc-2v1i »
      2toh »

Iron in PDB 2toh: Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat

Enzymatic activity of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat

All present enzymatic activity of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat:
1.14.16.2;

Protein crystallography data

The structure of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat, PDB code: 2toh was solved by K.E.Goodwill, C.Sabatier, R.C.Stevens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.30
Space group F 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 189.464, 148.595, 56.986, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 27.6

Other elements in 2toh:

The structure of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat (pdb code 2toh). 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 Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat, PDB code: 2toh:

Iron binding site 1 out of 1 in 2toh

Go back to Iron Binding Sites List in 2toh
Iron binding site 1 out of 1 in the Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:40.6
occ:1.00
 O A:HOH601 2.0 35.5 1.0
O A:HOH602 2.0 58.5 1.0
OE2 A:GLU376 2.0 37.4 1.0
NE2 A:HIS331 2.1 43.4 1.0
NE2 A:HIS336 2.2 39.2 1.0
OE1 A:GLU376 2.7 43.4 1.0
CD A:GLU376 2.7 38.2 1.0
CE1 A:HIS331 3.0 36.4 1.0
CE1 A:HIS336 3.1 40.2 1.0
CD2 A:HIS331 3.1 39.7 1.0
CD2 A:HIS336 3.2 33.8 1.0
O4 A:HBI500 3.6 89.2 1.0
CG A:GLU376 4.1 37.8 1.0
ND1 A:HIS331 4.2 37.6 1.0
ND1 A:HIS336 4.2 37.9 1.0
CG A:HIS331 4.3 40.8 1.0
CG A:HIS336 4.3 32.0 1.0
OE2 A:GLU332 4.4 42.1 1.0
CB A:ALA391 4.5 28.3 1.0
O A:HOH618 4.6 65.0 1.0
CB A:PRO327 4.8 58.3 1.0
C4 A:HBI500 4.8 91.2 1.0
OH A:TYR371 4.8 41.9 1.0
O10 A:HBI500 4.8 77.1 1.0

Reference:

K.E.Goodwill, C.Sabatier, R.C.Stevens. Crystal Structure of Tyrosine Hydroxylase with Bound Cofactor Analogue and Iron at 2.3 A Resolution: Self-Hydroxylation of PHE300 and the Pterin-Binding Site. Biochemistry V. 37 13437 1998.
ISSN: ISSN 0006-2960
PubMed: 9753429
DOI: 10.1021/BI981462G
Page generated: Sun Aug 4 02:19:59 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