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Iron in PDB 7lv1: Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II)

Protein crystallography data

The structure of Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II), PDB code: 7lv1 was solved by T.S.Choi, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.88 / 1.91
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 34.172, 83.211, 38.57, 90, 100.83, 90
R / Rfree (%) 19.1 / 23.7

Other elements in 7lv1:

The structure of Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) also contains other interesting chemical elements:

Calcium (Ca) 4 atoms
Copper (Cu) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) (pdb code 7lv1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II), PDB code: 7lv1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 7lv1

Go back to Iron Binding Sites List in 7lv1
Iron binding site 1 out of 2 in the Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe201

b:13.9
occ:1.00
FE C:HEC201 0.0 13.9 1.0
ND C:HEC201 2.0 8.1 1.0
NB C:HEC201 2.0 5.0 1.0
NC C:HEC201 2.1 8.2 1.0
NA C:HEC201 2.1 8.1 1.0
NE2 C:HIS102 2.2 9.7 1.0
SD C:MET7 2.5 7.5 1.0
C1D C:HEC201 3.0 7.4 1.0
C4D C:HEC201 3.0 11.2 1.0
C1B C:HEC201 3.1 7.5 1.0
C4B C:HEC201 3.1 7.8 1.0
C4A C:HEC201 3.1 10.6 1.0
CD2 C:HIS102 3.1 7.9 1.0
C4C C:HEC201 3.1 8.9 1.0
C1C C:HEC201 3.1 8.2 1.0
C1A C:HEC201 3.1 9.0 1.0
CE1 C:HIS102 3.2 9.3 1.0
CHD C:HEC201 3.4 7.8 1.0
CE C:MET7 3.4 7.4 1.0
CHB C:HEC201 3.4 8.0 1.0
CHC C:HEC201 3.4 6.0 1.0
CG C:MET7 3.5 5.7 1.0
CHA C:HEC201 3.5 10.9 1.0
C2D C:HEC201 4.2 8.6 1.0
C3D C:HEC201 4.2 8.2 1.0
CB C:MET7 4.2 7.5 1.0
CG C:HIS102 4.3 9.3 1.0
C2B C:HEC201 4.3 4.3 1.0
C3B C:HEC201 4.3 7.1 1.0
ND1 C:HIS102 4.3 10.9 1.0
C3A C:HEC201 4.3 11.1 1.0
C3C C:HEC201 4.3 6.7 1.0
C2A C:HEC201 4.3 12.9 1.0
C2C C:HEC201 4.3 9.7 1.0

Iron binding site 2 out of 2 in 7lv1

Go back to Iron Binding Sites List in 7lv1
Iron binding site 2 out of 2 in the Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cu-Bound Crystal Structure of the Engineered Cyt CB562 Variant, DICYT2, Crystallized in the Presence of Cu(II) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:16.1
occ:1.00
FE A:HEC201 0.0 16.1 1.0
ND A:HEC201 2.0 10.1 1.0
NA A:HEC201 2.0 11.9 1.0
NC A:HEC201 2.1 9.6 1.0
NB A:HEC201 2.1 8.0 1.0
NE2 A:HIS102 2.2 12.0 1.0
SD A:MET7 2.4 12.2 1.0
C1A A:HEC201 3.0 15.0 1.0
C4D A:HEC201 3.0 14.8 1.0
C1D A:HEC201 3.0 11.7 1.0
C4A A:HEC201 3.1 15.4 1.0
C4C A:HEC201 3.1 10.4 1.0
C1C A:HEC201 3.1 8.7 1.0
C4B A:HEC201 3.1 9.4 1.0
C1B A:HEC201 3.1 12.0 1.0
CD2 A:HIS102 3.2 11.0 1.0
CE1 A:HIS102 3.2 13.9 1.0
CHA A:HEC201 3.4 13.9 1.0
CE A:MET7 3.4 8.9 1.0
CG A:MET7 3.4 16.4 1.0
CHD A:HEC201 3.4 14.3 1.0
CHC A:HEC201 3.5 8.1 1.0
CHB A:HEC201 3.5 15.4 1.0
CB A:MET7 4.2 14.5 1.0
C2A A:HEC201 4.2 16.5 1.0
C2D A:HEC201 4.2 12.7 1.0
C3D A:HEC201 4.2 11.3 1.0
C3A A:HEC201 4.2 14.5 1.0
ND1 A:HIS102 4.3 12.2 1.0
CG A:HIS102 4.3 12.7 1.0
C2C A:HEC201 4.3 9.8 1.0
C3C A:HEC201 4.3 11.2 1.0
C2B A:HEC201 4.4 10.8 1.0
C3B A:HEC201 4.4 8.2 1.0
CA A:MET7 5.0 16.0 1.0

Reference:

T.S.Choi, F.A.Tezcan. Structure-Guided Metal Selectivity in Malleable Protein Interface Mediated By Single Disulfide Bond To Be Published.
Page generated: Thu Aug 8 07:13:30 2024

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