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Iron in PDB 6alm: Vioc L-Arginine Hydroxylase Bound to Fe(II), L-Arginine, and 2-Oxo- Glutaric Acid

Enzymatic activity of Vioc L-Arginine Hydroxylase Bound to Fe(II), L-Arginine, and 2-Oxo- Glutaric Acid

All present enzymatic activity of Vioc L-Arginine Hydroxylase Bound to Fe(II), L-Arginine, and 2-Oxo- Glutaric Acid:
1.14.11.41;

Protein crystallography data

The structure of Vioc L-Arginine Hydroxylase Bound to Fe(II), L-Arginine, and 2-Oxo- Glutaric Acid, PDB code: 6alm was solved by N.P.Dunham, A.J.Mitchell, A.K.Boal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.336, 66.990, 62.665, 90.00, 108.81, 90.00
R / Rfree (%) 19.8 / 23.1

Iron Binding Sites:

The binding sites of Iron atom in the Vioc L-Arginine Hydroxylase Bound to Fe(II), L-Arginine, and 2-Oxo- Glutaric Acid (pdb code 6alm). 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 Vioc L-Arginine Hydroxylase Bound to Fe(II), L-Arginine, and 2-Oxo- Glutaric Acid, PDB code: 6alm:

Iron binding site 1 out of 1 in 6alm

Go back to Iron Binding Sites List in 6alm
Iron binding site 1 out of 1 in the Vioc L-Arginine Hydroxylase Bound to Fe(II), L-Arginine, and 2-Oxo- Glutaric Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Vioc L-Arginine Hydroxylase Bound to Fe(II), L-Arginine, and 2-Oxo- Glutaric Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:12.6
occ:1.00
OE1 A:GLU170 2.0 15.7 1.0
O1 A:AKG402 2.0 18.9 1.0
NE2 A:HIS316 2.2 12.8 1.0
NE2 A:HIS168 2.3 13.6 1.0
O5 A:AKG402 2.4 18.2 1.0
C1 A:AKG402 2.9 18.7 1.0
C2 A:AKG402 3.0 18.1 1.0
CE1 A:HIS316 3.0 12.8 1.0
CD A:GLU170 3.0 15.8 1.0
CE1 A:HIS168 3.1 13.4 1.0
CD2 A:HIS316 3.1 12.6 1.0
CD2 A:HIS168 3.3 13.3 1.0
OE2 A:GLU170 3.4 16.9 1.0
N A:ARG403 3.9 25.8 1.0
ND1 A:HIS316 4.0 12.7 1.0
O2 A:AKG402 4.0 19.1 1.0
CG A:HIS316 4.1 12.5 1.0
ND1 A:HIS168 4.2 13.2 1.0
CG A:GLU170 4.3 15.1 1.0
CG A:HIS168 4.3 13.1 1.0
C3 A:AKG402 4.5 17.6 1.0
CG A:ARG403 4.7 24.9 1.0
CB A:GLU170 4.7 14.6 1.0
O A:HIS316 4.8 12.2 1.0
CB A:ARG403 4.8 25.4 1.0
CD2 A:LEU165 4.9 13.9 1.0
CA A:ARG403 4.9 25.6 1.0
CA A:GLU170 4.9 14.0 1.0
NE A:ARG334 5.0 15.1 0.6

Reference:

A.J.Mitchell, N.P.Dunham, R.J.Martinie, J.A.Bergman, C.J.Pollock, K.Hu, B.D.Allen, W.C.Chang, A.Silakov, J.M.Bollinger, C.Krebs, A.K.Boal. Visualizing the Reaction Cycle in An Iron(II)- and 2-(Oxo)-Glutarate-Dependent Hydroxylase. J. Am. Chem. Soc. V. 139 13830 2017.
ISSN: ESSN 1520-5126
PubMed: 28823155
DOI: 10.1021/JACS.7B07374
Page generated: Tue Aug 6 13:45:08 2024

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