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Iron in PDB 5xzi: Crystal Structure of the Zn-Directed Tetramer of the Engineered Cyt CB562 Variant, AB5

Protein crystallography data

The structure of Crystal Structure of the Zn-Directed Tetramer of the Engineered Cyt CB562 Variant, AB5, PDB code: 5xzi was solved by W.J.Song, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.67 / 2.65
Space group F 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 50.290, 98.000, 99.330, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 26.3

Other elements in 5xzi:

The structure of Crystal Structure of the Zn-Directed Tetramer of the Engineered Cyt CB562 Variant, AB5 also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms
Zinc (Zn) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Zn-Directed Tetramer of the Engineered Cyt CB562 Variant, AB5 (pdb code 5xzi). 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 Zn-Directed Tetramer of the Engineered Cyt CB562 Variant, AB5, PDB code: 5xzi:

Iron binding site 1 out of 1 in 5xzi

Go back to Iron Binding Sites List in 5xzi
Iron binding site 1 out of 1 in the Crystal Structure of the Zn-Directed Tetramer of the Engineered Cyt CB562 Variant, AB5


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 Zn-Directed Tetramer of the Engineered Cyt CB562 Variant, AB5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:52.0
occ:1.00
FE A:HEC201 0.0 52.0 1.0
ND A:HEC201 1.9 57.5 1.0
NA A:HEC201 2.0 62.7 1.0
NC A:HEC201 2.1 51.8 1.0
NB A:HEC201 2.1 60.0 1.0
NE2 A:HIS102 2.1 42.9 1.0
SD A:MET7 2.2 49.9 1.0
C1D A:HEC201 2.9 55.6 1.0
C4D A:HEC201 2.9 59.1 1.0
C1A A:HEC201 3.0 59.8 1.0
C4C A:HEC201 3.0 49.6 1.0
C4A A:HEC201 3.0 65.5 1.0
C1B A:HEC201 3.0 63.6 1.0
C4B A:HEC201 3.1 52.1 1.0
CE1 A:HIS102 3.1 42.8 1.0
C1C A:HEC201 3.1 49.1 1.0
CD2 A:HIS102 3.2 38.3 1.0
CG A:MET7 3.3 52.9 1.0
CHD A:HEC201 3.4 58.9 1.0
CHA A:HEC201 3.4 57.8 1.0
CHB A:HEC201 3.4 65.3 1.0
CHC A:HEC201 3.5 47.2 1.0
CE A:MET7 3.8 49.1 1.0
CB A:MET7 4.1 53.2 1.0
C2D A:HEC201 4.2 56.1 1.0
C3D A:HEC201 4.2 57.0 1.0
ND1 A:HIS102 4.2 41.3 1.0
C2A A:HEC201 4.2 66.1 1.0
C3A A:HEC201 4.2 63.1 1.0
C3C A:HEC201 4.3 49.2 1.0
C2C A:HEC201 4.3 48.1 1.0
CG A:HIS102 4.3 39.4 1.0
C2B A:HEC201 4.3 54.5 1.0
C3B A:HEC201 4.3 51.7 1.0
CA A:MET7 4.9 51.4 1.0

Reference:

W.J.Song, J.Yu, F.A.Tezcan. Importance of Scaffold Flexibility/Rigidity in the Design and Directed Evolution of Artificial Metallo-Beta-Lactamases. J. Am. Chem. Soc. V. 139 16772 2017.
ISSN: ESSN 1520-5126
PubMed: 28992705
DOI: 10.1021/JACS.7B08981
Page generated: Sun Dec 13 16:18:06 2020

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