Zinc in PDB 6egl: Crystal Structure of A De Novo Three-Stranded Coiled Coil Peptide Containing A D-Leu in the Second Coordination Sphere of A Non- Metalated Tris-Thiolate Binding Site

Protein crystallography data

The structure of Crystal Structure of A De Novo Three-Stranded Coiled Coil Peptide Containing A D-Leu in the Second Coordination Sphere of A Non- Metalated Tris-Thiolate Binding Site, PDB code: 6egl was solved by L.Ruckthong, J.A.Stuckey, V.L.Pecoraro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 9.28 / 1.40
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 38.213, 38.213, 140.655, 90.00, 90.00, 120.00
R / Rfree (%) 17.7 / 18.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A De Novo Three-Stranded Coiled Coil Peptide Containing A D-Leu in the Second Coordination Sphere of A Non- Metalated Tris-Thiolate Binding Site (pdb code 6egl). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of A De Novo Three-Stranded Coiled Coil Peptide Containing A D-Leu in the Second Coordination Sphere of A Non- Metalated Tris-Thiolate Binding Site, PDB code: 6egl:

Zinc binding site 1 out of 1 in 6egl

Go back to Zinc Binding Sites List in 6egl
Zinc binding site 1 out of 1 in the Crystal Structure of A De Novo Three-Stranded Coiled Coil Peptide Containing A D-Leu in the Second Coordination Sphere of A Non- Metalated Tris-Thiolate Binding Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of A De Novo Three-Stranded Coiled Coil Peptide Containing A D-Leu in the Second Coordination Sphere of A Non- Metalated Tris-Thiolate Binding Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn101

b:17.3
occ:0.85
OE1 A:GLU34 1.9 22.4 1.0
OE1 A:GLU31 2.0 17.5 1.0
NE2 A:HIS35 2.0 14.7 0.5
NE2 A:HIS35 2.0 23.3 0.5
CD2 A:HIS35 2.8 23.2 0.5
CD A:GLU31 2.9 19.1 1.0
HD2 A:HIS35 2.9 22.9 0.5
CD2 A:HIS35 3.0 14.3 0.5
CE1 A:HIS35 3.0 15.7 0.5
CD A:GLU34 3.0 22.5 1.0
OE2 A:GLU31 3.1 21.4 1.0
CE1 A:HIS35 3.1 24.1 0.5
HD2 A:HIS35 3.2 12.8 0.5
HG2 A:GLU34 3.2 23.9 1.0
HE1 A:HIS35 3.3 17.0 0.5
HB3 A:GLU34 3.5 18.7 1.0
HE1 A:HIS35 3.5 25.2 0.5
CG A:GLU34 3.6 23.2 1.0
HA A:GLU31 4.0 14.8 1.0
CG A:HIS35 4.0 22.8 0.5
OE2 A:GLU34 4.1 24.2 1.0
CG A:HIS35 4.1 14.9 0.5
ND1 A:HIS35 4.1 15.5 0.5
CB A:GLU34 4.1 20.2 1.0
ND1 A:HIS35 4.2 24.6 0.5
CG A:GLU31 4.2 16.9 1.0
HB3 A:GLU31 4.3 19.5 1.0
O A:HOH234 4.5 35.5 1.0
HG3 A:GLU34 4.6 23.8 1.0
HB2 A:GLU34 4.6 21.3 1.0
CB A:GLU31 4.7 16.2 1.0
HG3 A:GLU31 4.8 17.0 1.0
CA A:GLU31 4.8 15.3 1.0
HG2 A:GLU31 4.9 17.2 1.0

Reference:

L.Ruckthong, J.A.Stuckey, V.L.Pecoraro. How Outer Coordination Sphere Modifications Can Impact Metal Structures in Proteins: A Crystallographic Evaluation. Chemistry V. 25 6773 2019.
ISSN: ISSN 0947-6539
PubMed: 30861211
DOI: 10.1002/CHEM.201806040
Page generated: Wed Dec 16 11:42:57 2020

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