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Iron in PDB 3e2t: The Catalytic Domain of Chicken Tryptophan Hydroxylase 1 with Bound Tryptophan

Enzymatic activity of The Catalytic Domain of Chicken Tryptophan Hydroxylase 1 with Bound Tryptophan

All present enzymatic activity of The Catalytic Domain of Chicken Tryptophan Hydroxylase 1 with Bound Tryptophan:
1.14.16.4;

Protein crystallography data

The structure of The Catalytic Domain of Chicken Tryptophan Hydroxylase 1 with Bound Tryptophan, PDB code: 3e2t was solved by M.S.Windahl, C.R.Petersen, H.E.C.Christensen, P.Harris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.34 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 78.000, 155.300, 61.800, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 22.6

Iron Binding Sites:

The binding sites of Iron atom in the The Catalytic Domain of Chicken Tryptophan Hydroxylase 1 with Bound Tryptophan (pdb code 3e2t). 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 The Catalytic Domain of Chicken Tryptophan Hydroxylase 1 with Bound Tryptophan, PDB code: 3e2t:

Iron binding site 1 out of 1 in 3e2t

Go back to Iron Binding Sites List in 3e2t
Iron binding site 1 out of 1 in the The Catalytic Domain of Chicken Tryptophan Hydroxylase 1 with Bound Tryptophan


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Catalytic Domain of Chicken Tryptophan Hydroxylase 1 with Bound Tryptophan within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1

b:6.8
occ:1.00
N1 A:IMD2 1.9 15.8 1.0
NE2 A:HIS278 2.0 11.1 1.0
NE2 A:HIS273 2.1 6.4 1.0
OE2 A:GLU318 2.1 12.0 1.0
OE1 A:GLU318 2.7 12.0 1.0
CD A:GLU318 2.7 11.3 1.0
C2 A:IMD2 2.9 16.9 1.0
CE1 A:HIS278 3.0 10.9 1.0
CE1 A:HIS273 3.0 5.8 1.0
CD2 A:HIS278 3.0 9.5 1.0
C5 A:IMD2 3.0 17.5 1.0
CD2 A:HIS273 3.1 6.0 1.0
CZ3 A:TRP3 3.9 10.1 1.0
N3 A:IMD2 4.1 16.4 1.0
ND1 A:HIS278 4.1 10.7 1.0
ND1 A:HIS273 4.1 4.7 1.0
CB A:ALA333 4.1 6.3 1.0
CG A:HIS278 4.2 10.5 1.0
C4 A:IMD2 4.2 16.5 1.0
CG A:HIS273 4.2 6.6 1.0
CG A:GLU318 4.2 10.6 1.0
CE3 A:TRP3 4.6 10.1 1.0
OE2 A:GLU274 4.7 12.7 1.0
CH2 A:TRP3 4.7 10.4 1.0
CB A:GLU318 4.9 9.5 1.0

Reference:

M.S.Windahl, C.R.Petersen, H.E.M.Christensen, P.Harris. Crystal Structure of Tryptophan Hydroxylase with Bound Amino Acid Substrate Biochemistry V. 47 12087 2008.
ISSN: ISSN 0006-2960
PubMed: 18937498
DOI: 10.1021/BI8015263
Page generated: Sun Aug 4 09:19:13 2024

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