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Iron in PDB 8cvg: Structure of L289F Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, 2-Oxoglutarate, and 6-Oh-Hyoscyamine

Enzymatic activity of Structure of L289F Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, 2-Oxoglutarate, and 6-Oh-Hyoscyamine

All present enzymatic activity of Structure of L289F Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, 2-Oxoglutarate, and 6-Oh-Hyoscyamine:
1.14.11.11;

Protein crystallography data

The structure of Structure of L289F Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, 2-Oxoglutarate, and 6-Oh-Hyoscyamine, PDB code: 8cvg was solved by E.W.Wenger, A.K.Boal, J.M.Bollinger, C.Krebs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.57 / 1.56
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.719, 79.228, 55.822, 90, 111.03, 90
R / Rfree (%) 18.2 / 20.1

Other elements in 8cvg:

The structure of Structure of L289F Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, 2-Oxoglutarate, and 6-Oh-Hyoscyamine also contains other interesting chemical elements:

Strontium (Sr) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of L289F Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, 2-Oxoglutarate, and 6-Oh-Hyoscyamine (pdb code 8cvg). 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 Structure of L289F Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, 2-Oxoglutarate, and 6-Oh-Hyoscyamine, PDB code: 8cvg:

Iron binding site 1 out of 1 in 8cvg

Go back to Iron Binding Sites List in 8cvg
Iron binding site 1 out of 1 in the Structure of L289F Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, 2-Oxoglutarate, and 6-Oh-Hyoscyamine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of L289F Hyoscyamine 6-Beta Hydroxylase in Complex with Iron, 2-Oxoglutarate, and 6-Oh-Hyoscyamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:7.4
occ:1.00
 O1 A:AKG405 2.0 10.4 0.9
OD1 A:ASP219 2.1 7.5 1.0
NE2 A:HIS273 2.2 8.4 1.0
NE2 A:HIS217 2.2 8.7 1.0
O5 A:AKG405 2.2 11.2 0.9
O A:HOH520 2.4 16.2 1.0
C1 A:AKG405 2.9 10.7 0.9
C2 A:AKG405 2.9 10.7 0.9
CG A:ASP219 3.1 7.7 1.0
CD2 A:HIS273 3.1 8.4 1.0
CE1 A:HIS217 3.1 8.6 1.0
CD2 A:HIS217 3.1 8.6 1.0
CE1 A:HIS273 3.2 8.4 1.0
OD2 A:ASP219 3.3 7.6 1.0
O2 A:AKG405 4.0 10.9 0.9
CZ A:PHE289 4.1 8.3 1.0
O A:HOH713 4.2 19.2 1.0
ND1 A:HIS217 4.2 8.7 1.0
ND1 A:HIS273 4.3 8.4 1.0
CG A:HIS217 4.3 8.6 1.0
CG A:HIS273 4.3 8.5 1.0
C6 A:OVR409 4.3 9.7 1.0
C3 A:AKG405 4.3 10.3 0.9
O1 A:OVR409 4.4 9.6 1.0
CB A:ASP219 4.4 7.7 1.0
N A:ASP219 4.8 8.0 1.0
CA A:ASP219 4.8 7.9 1.0
CE1 A:PHE289 4.8 8.3 1.0
C4 A:AKG405 4.9 9.8 0.9
C7 A:OVR409 4.9 9.7 1.0
CE2 A:PHE289 5.0 8.4 1.0

Reference:

E.S.Wenger, A.K.Boal, J.M.Bollinger, C.Krebs. Structure of the L289F H6H Cyclization Reactant Complex To Be Published.
Page generated: Fri Aug 9 23:02:57 2024

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