Iron in PDB 8sfc: Crystal Structure of the Engineered Ssopox Variant IVA4 in Alternate State

Enzymatic activity of Crystal Structure of the Engineered Ssopox Variant IVA4 in Alternate State

All present enzymatic activity of Crystal Structure of the Engineered Ssopox Variant IVA4 in Alternate State:
3.1.8.1;

Protein crystallography data

The structure of Crystal Structure of the Engineered Ssopox Variant IVA4 in Alternate State, PDB code: 8sfc was solved by P.Jacquet, R.Billot, A.Shimon, N.Hoekstra, C.Bergonzi, A.Jenks, D.Daude, M.H.Elias, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.48 / 1.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 64.09, 74.95, 137.11, 90, 90, 90
R / Rfree (%) 20.5 / 22.6

Other elements in 8sfc:

The structure of Crystal Structure of the Engineered Ssopox Variant IVA4 in Alternate State also contains other interesting chemical elements:

Cobalt (Co) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Engineered Ssopox Variant IVA4 in Alternate State (pdb code 8sfc). 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 Engineered Ssopox Variant IVA4 in Alternate State, PDB code: 8sfc:

Iron binding site 1 out of 1 in 8sfc

Go back to Iron Binding Sites List in 8sfc
Iron binding site 1 out of 1 in the Crystal Structure of the Engineered Ssopox Variant IVA4 in Alternate State


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 Engineered Ssopox Variant IVA4 in Alternate State within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe401

b:27.7
occ:0.74
 OQ1 D:KCX137 2.0 45.2 1.0
NE2 D:HIS24 2.0 27.6 0.5
NE2 D:HIS22 2.3 28.3 1.0
OD2 D:ASP256 2.7 43.3 0.6
CX D:KCX137 2.8 46.8 1.0
CE1 D:HIS24 2.9 29.6 0.5
CD2 D:HIS24 3.0 30.4 0.5
CD2 D:HIS22 3.1 26.5 1.0
OQ2 D:KCX137 3.1 42.3 1.0
CE1 D:HIS22 3.3 30.4 1.0
CG D:ASP256 3.7 47.6 0.6
N D:CYS259 3.7 34.2 0.6
CO D:CO402 3.8 28.1 0.9
NZ D:KCX137 3.8 25.9 1.0
CA D:CYS258 4.0 38.5 0.6
ND1 D:HIS24 4.0 22.5 0.5
CG D:HIS24 4.1 26.2 0.5
CE1 D:HIS199 4.2 46.2 1.0
NE2 D:HIS199 4.3 47.4 1.0
CB D:ASP256 4.3 42.5 0.6
CG D:PRO67 4.3 28.5 1.0
CG D:HIS22 4.3 27.4 1.0
C D:CYS258 4.4 36.2 0.6
O D:TYR257 4.4 43.9 0.7
ND1 D:HIS22 4.4 35.3 1.0
SG D:CYS259 4.4 39.0 0.6
CB D:CYS259 4.5 29.4 0.6
OD1 D:ASP256 4.5 45.9 0.6
CA D:CYS259 4.7 32.2 0.6
SG D:CYS258 4.8 27.8 0.6
N D:CYS258 4.8 40.2 0.6
C D:TYR257 4.9 43.1 0.7
CB D:CYS258 4.9 37.7 0.6

Reference:

P.Jacquet, R.Billot, A.Shimon, N.Hoekstra, C.Bergonzi, A.Jenks, E.Chabriere, D.Daude, M.H.Elias. Changes in Active Site Loops Conformation Relates to A Transition From Lactonase to Phosphotriesterase To Be Published.
Page generated: Sat Aug 10 17:46:10 2024

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