Atomistry » Zinc » PDB 3boc-3c4u » 3bvz
Atomistry »
  Zinc »
    PDB 3boc-3c4u »
      3bvz »

Zinc in PDB 3bvz: Manipulating the Coupled Folding and Binding Process Drives Affinity Maturation in A Protein-Protein Complex

Protein crystallography data

The structure of Manipulating the Coupled Folding and Binding Process Drives Affinity Maturation in A Protein-Protein Complex, PDB code: 3bvz was solved by S.Cho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 42.596, 42.596, 287.418, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 27.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Manipulating the Coupled Folding and Binding Process Drives Affinity Maturation in A Protein-Protein Complex (pdb code 3bvz). 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 Manipulating the Coupled Folding and Binding Process Drives Affinity Maturation in A Protein-Protein Complex, PDB code: 3bvz:

Zinc binding site 1 out of 1 in 3bvz

Go back to Zinc Binding Sites List in 3bvz
Zinc binding site 1 out of 1 in the Manipulating the Coupled Folding and Binding Process Drives Affinity Maturation in A Protein-Protein Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Manipulating the Coupled Folding and Binding Process Drives Affinity Maturation in A Protein-Protein Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn240

b:22.8
occ:1.00
NE2 A:HIS122 2.0 13.5 1.0
OD2 A:ASP83 2.1 14.9 1.0
ND1 A:HIS118 2.3 11.7 1.0
CG A:ASP83 2.7 10.9 1.0
OD1 A:ASP83 2.8 9.6 1.0
CE1 A:HIS122 2.9 14.7 1.0
CD2 A:HIS122 3.1 14.3 1.0
CE1 A:HIS118 3.1 12.4 1.0
CG A:HIS118 3.5 15.0 1.0
CB A:HIS118 3.9 16.3 1.0
CA A:HIS118 3.9 17.6 1.0
O A:HOH286 4.0 10.2 1.0
ND1 A:HIS122 4.1 14.8 1.0
O A:HIS118 4.1 18.1 1.0
CG A:HIS122 4.2 16.9 1.0
CB A:ASP83 4.2 10.4 1.0
NE2 A:HIS118 4.3 15.8 1.0
C A:HIS118 4.5 18.8 1.0
CD2 A:HIS118 4.5 16.0 1.0
CG A:LYS37 4.6 23.5 1.0
N A:LYS37 5.0 21.9 1.0

Reference:

S.Cho, C.P.Swaminathan, M.C.Kerzic, R.Guan, J.Yang, M.C.Kieke, P.S.Andersen, D.M.Krantz, R.A.Mariuzza, S.J.Eric. Manipulating the Coupled Folding and Binding Process Drives Affinity Maturation in A Protein-Protein Complex To Be Published.
Page generated: Thu Oct 24 11:38:53 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy