Iron in PDB 9eqf: Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate

Enzymatic activity of Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate

All present enzymatic activity of Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate:
1.14.11.41;

Protein crystallography data

The structure of Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate, PDB code: 9eqf was solved by F.J.Hardy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.48 / 1.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 81.145, 67.107, 62.945, 90, 109.22, 90
R / Rfree (%) 15.8 / 18.7

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate (pdb code 9eqf). 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 the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate, PDB code: 9eqf:

Iron binding site 1 out of 1 in 9eqf

Go back to Iron Binding Sites List in 9eqf
Iron binding site 1 out of 1 in the Crystal Structure of the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate


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 the L-Arginine Hydroxylase Vioc MEHIS316, Bound to Fe(II), L-Arginine, and Succinate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:19.3
occ:0.30
 NE2 A:MHS316 1.7 39.8 1.0
CE1 A:MHS316 2.2 30.2 1.0
OE1 A:GLU170 2.2 28.4 1.0
HE1 A:MHS316 2.2 36.2 1.0
O4 A:SIN402 2.4 47.6 0.8
NE2 A:HIS168 2.8 32.7 1.0
CD2 A:MHS316 2.9 31.9 1.0
C4 A:SIN402 3.1 30.3 0.8
O3 A:SIN402 3.2 39.6 0.8
HE1 A:HIS168 3.3 32.6 1.0
CE1 A:HIS168 3.3 27.1 1.0
CD A:GLU170 3.4 31.4 1.0
ND1 A:MHS316 3.4 28.8 1.0
HD2 A:MHS316 3.4 38.3 1.0
CG A:MHS316 3.7 23.9 1.0
N A:ARG403 3.8 33.1 0.8
HH11 A:ARG334 3.8 44.3 1.0
CD2 A:HIS168 3.9 25.2 1.0
HB2 A:GLU170 3.9 21.9 1.0
OE2 A:GLU170 3.9 31.8 1.0
HD21 A:LEU165 4.1 23.2 1.0
HD2 A:HIS168 4.2 30.3 1.0
HG11 A:VAL181 4.3 22.5 1.0
HA A:GLU170 4.3 20.6 1.0
HH12 A:ARG334 4.3 44.3 1.0
NH1 A:ARG334 4.4 36.9 1.0
ND1 A:HIS168 4.4 25.4 1.0
C3 A:SIN402 4.5 17.8 0.8
CM A:MHS316 4.5 29.7 1.0
HM1 A:MHS316 4.5 35.7 1.0
CG A:GLU170 4.5 16.0 1.0
CB A:GLU170 4.5 18.2 1.0
HG2 A:ARG403 4.6 42.3 0.8
H22 A:SIN402 4.6 25.6 0.8
O A:MHS316 4.7 15.3 1.0
HG21 A:VAL181 4.7 26.2 1.0
H32 A:SIN402 4.7 21.4 0.8
HD23 A:LEU165 4.7 23.2 1.0
CG A:HIS168 4.7 20.5 1.0
HM2 A:MHS316 4.8 35.7 1.0
CD2 A:LEU165 4.9 19.3 1.0
CA A:GLU170 4.9 17.1 1.0
HD2 A:ARG334 4.9 27.3 1.0
HB2 A:ARG403 4.9 49.1 0.8
HG2 A:GLU170 5.0 19.2 1.0

Reference:

F.J.Hardy, M.G.Quesne, E.F.Gerard, J.Zhao, M.Ortmayer, C.J.Taylor, H.S.Ali, J.W.Slater, C.W.Levy, D.J.Heyes, J.M.J.Bollinger, S.P.De Visser, A.P.Green. Probing Ferryl Reactivity in A Nonheme Iron Oxygenase Using An Expanded Genetic Code Acs Catalysis 11584 2024.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.4C02365
Page generated: Sun Aug 11 12:05:45 2024

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