Iron in PDB 7abb: The Truncated Structure of the Bottromycin Biosynthetic Protein Salcyp

Protein crystallography data

The structure of The Truncated Structure of the Bottromycin Biosynthetic Protein Salcyp, PDB code: 7abb was solved by S.Adam, J.Koehnke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.27 / 1.50
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 96.538, 96.538, 49.999, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 18.1

Iron Binding Sites:

The binding sites of Iron atom in the The Truncated Structure of the Bottromycin Biosynthetic Protein Salcyp (pdb code 7abb). 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 The Truncated Structure of the Bottromycin Biosynthetic Protein Salcyp, PDB code: 7abb:

Iron binding site 1 out of 1 in 7abb

Go back to Iron Binding Sites List in 7abb
Iron binding site 1 out of 1 in the The Truncated Structure of the Bottromycin Biosynthetic Protein Salcyp


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Truncated Structure of the Bottromycin Biosynthetic Protein Salcyp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:17.5
occ:1.00
FE A:HEC501 0.0 17.5 1.0
ND A:HEC501 2.0 16.0 1.0
NB A:HEC501 2.0 15.9 1.0
NA A:HEC501 2.0 17.1 1.0
NC A:HEC501 2.0 17.6 1.0
SG A:CYS354 2.3 17.9 1.0
HG A:CYS354 2.5 21.5 1.0
C1D A:HEC501 3.0 18.9 1.0
C4D A:HEC501 3.0 18.5 1.0
C1B A:HEC501 3.0 17.4 1.0
C4B A:HEC501 3.0 16.6 1.0
C1C A:HEC501 3.0 17.2 1.0
C4A A:HEC501 3.1 15.6 1.0
C4C A:HEC501 3.1 17.1 1.0
C1A A:HEC501 3.1 17.3 1.0
HB2 A:CYS354 3.1 21.0 1.0
CB A:CYS354 3.3 17.5 1.0
CHD A:HEC501 3.4 18.7 1.0
CHB A:HEC501 3.4 15.3 1.0
CHC A:HEC501 3.4 16.8 1.0
CHA A:HEC501 3.4 17.9 1.0
HA A:CYS354 3.6 21.8 1.0
HB1 A:ALA247 3.9 27.3 1.0
H A:GLY356 3.9 21.4 1.0
CA A:CYS354 4.0 18.1 1.0
HB3 A:CYS354 4.1 21.0 1.0
C2D A:HEC501 4.2 19.3 1.0
C2B A:HEC501 4.2 17.4 1.0
C3B A:HEC501 4.2 16.6 1.0
C3D A:HEC501 4.3 20.4 1.0
C2C A:HEC501 4.3 16.8 1.0
C3A A:HEC501 4.3 18.9 1.0
C3C A:HEC501 4.3 17.1 1.0
HD1 A:PHE347 4.3 20.3 1.0
C2A A:HEC501 4.3 18.4 1.0
HHD A:HEC501 4.4 22.5 1.0
H A:LEU355 4.4 22.9 1.0
HHB A:HEC501 4.4 18.3 1.0
HHC A:HEC501 4.4 20.1 1.0
HHA A:HEC501 4.4 21.4 1.0
O A:ALA247 4.7 25.4 1.0
C A:CYS354 4.7 19.7 1.0
N A:GLY356 4.7 17.8 1.0
HA3 A:GLY356 4.7 21.2 1.0
N A:LEU355 4.7 19.1 1.0
CB A:ALA247 4.8 22.8 1.0
HE1 A:MET294 5.0 42.8 1.0

Reference:

S.Adam, J.Koehnke. The Structure of the Bottromycin Biosynthetic Protein Salcyp J.Am.Chem.Soc. 2020.
ISSN: ESSN 1520-5126
DOI: 10.1021/JACS.0C10361
Page generated: Sun Dec 13 18:34:47 2020

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