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Zinc in PDB 2psr: Human Psoriasin (S100A7) CA2+ and ZN2+ Bound Form (Crystal Form II)

Protein crystallography data

The structure of Human Psoriasin (S100A7) CA2+ and ZN2+ Bound Form (Crystal Form II), PDB code: 2psr was solved by D.E.Brodersen, J.Nyborg, M.Kjeldgaard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 2.05
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 51.958, 51.958, 116.027, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 26.5

Other elements in 2psr:

The structure of Human Psoriasin (S100A7) CA2+ and ZN2+ Bound Form (Crystal Form II) also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Psoriasin (S100A7) CA2+ and ZN2+ Bound Form (Crystal Form II) (pdb code 2psr). 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 Human Psoriasin (S100A7) CA2+ and ZN2+ Bound Form (Crystal Form II), PDB code: 2psr:

Zinc binding site 1 out of 1 in 2psr

Go back to Zinc Binding Sites List in 2psr
Zinc binding site 1 out of 1 in the Human Psoriasin (S100A7) CA2+ and ZN2+ Bound Form (Crystal Form II)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Psoriasin (S100A7) CA2+ and ZN2+ Bound Form (Crystal Form II) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn103

b:20.9
occ:1.00
NE2 A:HIS90 1.9 20.5 1.0
NE2 A:HIS86 2.1 22.1 1.0
CD2 A:HIS90 2.9 19.7 1.0
CE1 A:HIS90 3.0 22.4 1.0
CD2 A:HIS86 3.0 15.0 1.0
CE1 A:HIS86 3.0 18.5 1.0
ND1 A:HIS90 4.0 21.5 1.0
CG A:HIS90 4.0 20.6 1.0
ND1 A:HIS86 4.1 22.9 1.0
CG A:HIS86 4.1 26.1 1.0
OG A:SER89 4.7 22.9 1.0

Reference:

D.E.Brodersen, J.Nyborg, M.Kjeldgaard. Zinc-Binding Site of An S100 Protein Revealed. Two Crystal Structures of CA2+-Bound Human Psoriasin (S100A7) in the ZN2+-Loaded and ZN2+-Free States. Biochemistry V. 38 1695 1999.
ISSN: ISSN 0006-2960
PubMed: 10026247
DOI: 10.1021/BI982483D
Page generated: Wed Dec 16 03:49:00 2020

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