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Zinc in PDB 1au1: Human Interferon-Beta Crystal Structure

Protein crystallography data

The structure of Human Interferon-Beta Crystal Structure, PDB code: 1au1 was solved by M.Karpusas, M.Nolte, W.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.300, 65.900, 121.500, 90.00, 90.00, 90.00
R / Rfree (%) 22.3 / 28.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Interferon-Beta Crystal Structure (pdb code 1au1). 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 Interferon-Beta Crystal Structure, PDB code: 1au1:

Zinc binding site 1 out of 1 in 1au1

Go back to Zinc Binding Sites List in 1au1
Zinc binding site 1 out of 1 in the Human Interferon-Beta Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Interferon-Beta Crystal Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn169

b:46.1
occ:1.00
NE2 B:HIS93 1.6 36.1 1.0
H1 B:HOH221 2.0 0.0 1.0
NE2 A:HIS121 2.0 29.9 1.0
NE2 B:HIS97 2.0 25.8 1.0
CE1 B:HIS93 2.3 36.5 1.0
H2 B:HOH221 2.6 0.0 1.0
CE1 A:HIS121 2.7 30.5 1.0
O B:HOH221 2.7 43.0 1.0
CE1 B:HIS97 2.7 28.1 1.0
CD2 B:HIS93 2.9 34.4 1.0
CD2 A:HIS121 3.2 29.9 1.0
CD2 B:HIS97 3.2 27.5 1.0
ND1 B:HIS93 3.5 35.0 1.0
HH12 A:ARG124 3.5 0.0 1.0
CG B:HIS93 3.8 33.2 1.0
HH22 A:ARG124 3.9 0.0 1.0
ND1 A:HIS121 3.9 32.2 1.0
ND1 B:HIS97 4.0 26.9 1.0
CG A:HIS121 4.2 30.8 1.0
CG B:HIS97 4.2 26.4 1.0
HD1 B:HIS93 4.3 0.0 1.0
NH1 A:ARG124 4.5 99.7 1.0
HD22 B:ASN96 4.7 0.0 1.0
HD1 A:HIS121 4.7 0.0 1.0
HD1 B:HIS97 4.7 0.0 1.0
CD1 A:LEU120 4.8 35.2 1.0
NH2 A:ARG124 4.8 99.7 1.0
O B:HIS93 4.9 30.0 1.0
CB A:LEU120 5.0 43.5 1.0

Reference:

M.Karpusas, M.Nolte, C.B.Benton, W.Meier, W.N.Lipscomb, S.Goelz. The Crystal Structure of Human Interferon Beta at 2.2-A Resolution. Proc.Natl.Acad.Sci.Usa V. 94 11813 1997.
ISSN: ISSN 0027-8424
PubMed: 9342320
DOI: 10.1073/PNAS.94.22.11813
Page generated: Sat Oct 12 22:16:31 2024

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