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Zinc in PDB 3czt: Crystal Structure of S100B in the Calcium and Zinc Loaded State at pH 9

Protein crystallography data

The structure of Crystal Structure of S100B in the Calcium and Zinc Loaded State at pH 9, PDB code: 3czt was solved by T.Ostendorp, J.Diez, C.W.Heizmann, G.Fritz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.80 / 1.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 34.980, 89.260, 59.580, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 22.2

Other elements in 3czt:

The structure of Crystal Structure of S100B in the Calcium and Zinc Loaded State at pH 9 also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of S100B in the Calcium and Zinc Loaded State at pH 9 (pdb code 3czt). 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 S100B in the Calcium and Zinc Loaded State at pH 9, PDB code: 3czt:

Zinc binding site 1 out of 1 in 3czt

Go back to Zinc Binding Sites List in 3czt
Zinc binding site 1 out of 1 in the Crystal Structure of S100B in the Calcium and Zinc Loaded State at pH 9


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 S100B in the Calcium and Zinc Loaded State at pH 9 within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Zn95

b:20.5
occ:1.00
NE2 X:HIS90 1.9 24.1 1.0
NE2 X:HIS85 2.1 16.3 1.0
CD2 X:HIS90 2.8 22.3 1.0
CE1 X:HIS90 2.9 23.6 1.0
CD2 X:HIS85 3.1 16.4 1.0
CE1 X:HIS85 3.1 16.0 1.0
O X:HOH263 3.3 43.5 1.0
CG X:HIS90 4.0 25.3 1.0
ND1 X:HIS90 4.0 24.3 1.0
CG X:HIS85 4.2 17.3 1.0
ND1 X:HIS85 4.2 16.9 1.0
O X:HOH206 4.7 26.7 1.0

Reference:

T.Ostendorp, J.Diez, C.W.Heizmann, G.Fritz. The Crystal Structures of Human S100B in the Zinc- and Calcium-Loaded State at Three pH Values Reveal Zinc Ligand Swapping. Biochim.Biophys.Acta V.1813 1083 2011.
ISSN: ISSN 0006-3002
PubMed: 20950652
DOI: 10.1016/J.BBAMCR.2010.10.006
Page generated: Wed Dec 16 04:11:36 2020

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