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Iron in PDB 1mlw: Crystal Structure of Human Tryptophan Hydroxylase with Bound 7,8-Dihydro-L-Biopterin Cofactor and Fe(III)

Enzymatic activity of Crystal Structure of Human Tryptophan Hydroxylase with Bound 7,8-Dihydro-L-Biopterin Cofactor and Fe(III)

All present enzymatic activity of Crystal Structure of Human Tryptophan Hydroxylase with Bound 7,8-Dihydro-L-Biopterin Cofactor and Fe(III):
1.14.16.4;

Protein crystallography data

The structure of Crystal Structure of Human Tryptophan Hydroxylase with Bound 7,8-Dihydro-L-Biopterin Cofactor and Fe(III), PDB code: 1mlw was solved by L.Wang, H.Erlandsen, J.Haavik, P.M.Knappskog, R.C.Stevens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.71
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.775, 57.334, 109.410, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 23

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Human Tryptophan Hydroxylase with Bound 7,8-Dihydro-L-Biopterin Cofactor and Fe(III) (pdb code 1mlw). 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 Tryptophan Hydroxylase with Bound 7,8-Dihydro-L-Biopterin Cofactor and Fe(III), PDB code: 1mlw:

Iron binding site 1 out of 1 in 1mlw

Go back to Iron Binding Sites List in 1mlw
Iron binding site 1 out of 1 in the Crystal Structure of Human Tryptophan Hydroxylase with Bound 7,8-Dihydro-L-Biopterin Cofactor and Fe(III)


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 Tryptophan Hydroxylase with Bound 7,8-Dihydro-L-Biopterin Cofactor and Fe(III) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe403

b:21.4
occ:1.00
 NE2 A:HIS277 2.0 21.5 1.0
NE2 A:HIS272 2.1 19.6 1.0
O A:HOH602 2.1 21.0 1.0
O A:HOH600 2.2 21.0 1.0
O A:HOH601 2.2 21.0 1.0
OE2 A:GLU317 2.4 32.4 1.0
CD2 A:HIS277 3.0 24.0 1.0
CE1 A:HIS277 3.0 21.8 1.0
CE1 A:HIS272 3.0 17.4 1.0
CD2 A:HIS272 3.1 17.8 1.0
CD A:GLU317 3.3 28.2 1.0
OE1 A:GLU317 3.4 30.9 1.0
O4 A:HBI900 3.6 33.9 1.0
OH A:TYR235 4.0 44.1 1.0
ND1 A:HIS277 4.1 23.9 1.0
CG A:HIS277 4.1 23.0 1.0
O A:HOH719 4.2 36.9 1.0
ND1 A:HIS272 4.2 18.5 1.0
O A:HOH725 4.2 34.5 1.0
CG A:HIS272 4.2 19.7 1.0
OE2 A:GLU273 4.4 18.3 1.0
CB A:ALA332 4.6 16.2 1.0
CG A:GLU317 4.7 27.1 1.0
C4 A:HBI900 4.8 30.2 1.0
CZ A:TYR235 4.9 43.8 1.0
CZ A:PHE250 5.0 24.3 1.0

Reference:

L.Wang, H.Erlandsen, J.Haavik, P.M.Knappskog, R.C.Stevens. Three-Dimensional Structure of Human Tryptophan Hydroxylase and Its Implications For the Biosynthesis of the Neurotransmitters Serotonin and Melatonin Biochemistry V. 41 12569 2002.
ISSN: ISSN 0006-2960
PubMed: 12379098
DOI: 10.1021/BI026561F
Page generated: Sat Aug 3 11:01:55 2024

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