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Iron in PDB 1ltv: Crystal Structure of Chromobacterium Violaceum Phenylalanine Hydroxylase, Structure with Bound Oxidized Fe(III)

Enzymatic activity of Crystal Structure of Chromobacterium Violaceum Phenylalanine Hydroxylase, Structure with Bound Oxidized Fe(III)

All present enzymatic activity of Crystal Structure of Chromobacterium Violaceum Phenylalanine Hydroxylase, Structure with Bound Oxidized Fe(III):
1.14.16.1;

Protein crystallography data

The structure of Crystal Structure of Chromobacterium Violaceum Phenylalanine Hydroxylase, Structure with Bound Oxidized Fe(III), PDB code: 1ltv was solved by H.Erlandsen, J.Y.Kim, M.G.Patch, A.Han, A.Volner, M.M.Abu-Omar, R.C.Stevens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.594, 67.533, 90.847, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 26.1

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Chromobacterium Violaceum Phenylalanine Hydroxylase, Structure with Bound Oxidized Fe(III) (pdb code 1ltv). 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 Chromobacterium Violaceum Phenylalanine Hydroxylase, Structure with Bound Oxidized Fe(III), PDB code: 1ltv:

Iron binding site 1 out of 1 in 1ltv

Go back to Iron Binding Sites List in 1ltv
Iron binding site 1 out of 1 in the Crystal Structure of Chromobacterium Violaceum Phenylalanine Hydroxylase, Structure with Bound Oxidized 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 Chromobacterium Violaceum Phenylalanine Hydroxylase, Structure with Bound Oxidized Fe(III) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe900

b:26.8
occ:1.00
 O A:HOH582 2.0 28.8 1.0
NE2 A:HIS138 2.0 20.5 1.0
OE2 A:GLU184 2.2 23.4 1.0
NE2 A:HIS143 2.4 18.1 1.0
O A:HOH583 2.4 28.8 1.0
OE1 A:GLU184 2.5 18.7 1.0
CD A:GLU184 2.6 20.9 1.0
CE1 A:HIS138 2.9 19.6 1.0
CD2 A:HIS138 3.1 18.3 1.0
CD2 A:HIS143 3.3 15.7 1.0
CE1 A:HIS143 3.3 16.3 1.0
O A:HOH473 3.5 28.8 1.0
O A:HOH506 3.9 36.2 1.0
OD1 A:ASP139 4.0 21.7 1.0
ND1 A:HIS138 4.1 21.8 1.0
CG A:GLU184 4.1 15.9 1.0
CG A:HIS138 4.2 19.1 1.0
OH A:TYR130 4.3 0.3 1.0
ND1 A:HIS143 4.4 18.1 1.0
CG A:HIS143 4.5 17.0 1.0
CB A:ALA199 4.6 16.9 1.0
CG A:PRO134 4.9 46.6 1.0
CB A:PRO134 5.0 44.4 1.0
CB A:GLU184 5.0 14.7 1.0

Reference:

H.Erlandsen, J.Y.Kim, M.G.Patch, A.Han, A.Volner, M.M.Abu-Omar, R.C.Stevens. Structural Comparison of Bacterial and Human Iron-Dependent Phenylalanine Hydroxylases: Similar Fold, Different Stability and Reaction Rates. J.Mol.Biol. V. 320 645 2002.
ISSN: ISSN 0022-2836
PubMed: 12096915
DOI: 10.1016/S0022-2836(02)00496-5
Page generated: Sat Aug 3 09:55:17 2024

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