Zinc in PDB 1jmu: Crystal Structure of the Reovirus MU1/SIGMA3 Complex

The structure of Crystal Structure of the Reovirus MU1/SIGMA3 Complex, PDB code: 1jmu was solved by S.Liemann, M.L.Nibert, S.C.Harrison, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 2.80
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	180.294, 184.942, 284.324, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 24.1

The structure of Crystal Structure of the Reovirus MU1/SIGMA3 Complex also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Crystal Structure of the Reovirus MU1/SIGMA3 Complex (pdb code 1jmu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the Reovirus MU1/SIGMA3 Complex, PDB code: 1jmu:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of the Reovirus MU1/SIGMA3 Complex


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 the Reovirus MU1/SIGMA3 Complex within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn702 b:39.7 occ:1.00 NE2 G:HIS71 1.9 42.5 1.0 SG G:CYS54 2.3 45.3 1.0 SG G:CYS73 2.3 42.4 1.0 SG G:CYS51 2.3 41.8 1.0 CE1 G:HIS71 2.8 43.5 1.0 CB G:CYS73 3.0 45.4 1.0 CD2 G:HIS71 3.1 42.5 1.0 CB G:CYS51 3.2 41.4 1.0 CB G:CYS54 3.4 44.9 1.0 N G:CYS54 3.7 43.9 1.0 CA G:CYS73 3.8 47.3 1.0 ND1 G:HIS71 3.9 44.2 1.0 CB G:HIS53 4.1 46.5 1.0 CA G:CYS54 4.1 43.4 1.0 CG G:HIS71 4.1 43.7 1.0 C G:HIS53 4.2 45.1 1.0 CA G:HIS53 4.5 44.6 1.0 N G:HIS53 4.6 44.2 1.0 CA G:CYS51 4.6 41.5 1.0 C G:CYS73 4.7 47.8 1.0 N G:CYS73 4.8 47.6 1.0 C G:CYS51 4.8 41.8 1.0 O G:CYS51 4.9 42.3 1.0 O G:HIS53 4.9 45.6 1.0 C G:CYS54 4.9 42.8 1.0 N G:ASN74 5.0 48.1 1.0 N G:LEU55 5.0 42.2 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of the Reovirus MU1/SIGMA3 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Reovirus MU1/SIGMA3 Complex within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn703 b:45.6 occ:1.00 NE2 H:HIS71 1.9 40.2 1.0 SG H:CYS51 2.2 40.4 1.0 SG H:CYS54 2.3 42.8 1.0 SG H:CYS73 2.3 46.3 1.0 CE1 H:HIS71 2.7 40.1 1.0 CB H:CYS51 3.1 41.9 1.0 CD2 H:HIS71 3.1 42.1 1.0 CB H:CYS73 3.1 47.4 1.0 CB H:CYS54 3.4 43.6 1.0 N H:CYS54 3.7 45.4 1.0 CA H:CYS73 3.9 48.0 1.0 ND1 H:HIS71 3.9 40.7 1.0 CB H:HIS53 4.1 48.8 1.0 CG H:HIS71 4.1 41.7 1.0 CA H:CYS54 4.1 45.0 1.0 C H:HIS53 4.2 45.7 1.0 CA H:CYS51 4.5 43.0 1.0 CA H:HIS53 4.5 45.9 1.0 N H:HIS53 4.5 46.3 1.0 C H:CYS51 4.8 43.8 1.0 C H:CYS73 4.8 48.3 1.0 O H:CYS51 4.9 43.7 1.0 C H:CYS54 4.9 45.0 1.0 N H:CYS73 4.9 47.7 1.0 O H:HIS53 4.9 45.4 1.0 N H:LEU55 5.0 44.9 1.0 O H:HOH722 5.0 47.6 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of the Reovirus MU1/SIGMA3 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Reovirus MU1/SIGMA3 Complex within 5.0Å range: probe atom residue distance (Å) B Occ I:Zn701 b:52.6 occ:1.00 NE2 I:HIS71 2.0 43.7 1.0 SG I:CYS51 2.3 43.6 1.0 SG I:CYS54 2.3 43.0 1.0 SG I:CYS73 2.3 47.7 1.0 CE1 I:HIS71 2.8 41.9 1.0 CB I:CYS73 3.1 48.4 1.0 CB I:CYS51 3.1 42.4 1.0 CD2 I:HIS71 3.2 44.1 1.0 CB I:CYS54 3.4 44.5 1.0 N I:CYS54 3.6 45.6 1.0 CA I:CYS73 3.9 49.5 1.0 CB I:HIS53 4.0 48.4 1.0 ND1 I:HIS71 4.0 43.2 1.0 CA I:CYS54 4.1 44.7 1.0 C I:HIS53 4.1 45.9 1.0 CG I:HIS71 4.2 43.8 1.0 CA I:HIS53 4.4 46.6 1.0 N I:HIS53 4.5 46.4 1.0 CA I:CYS51 4.5 42.5 1.0 C I:CYS51 4.8 43.6 1.0 C I:CYS73 4.8 50.0 1.0 O I:CYS51 4.8 45.2 1.0 O I:HIS53 4.9 46.0 1.0 C I:CYS54 4.9 44.6 1.0 N I:CYS73 4.9 49.4 1.0 N I:LEU55 4.9 44.0 1.0

S.Liemann, K.Chandran, T.S.Baker, M.L.Nibert, S.C.Harrison. Structure of the Reovirus Membrane-Penetration Protein, MU1, in A Complex with Is Protector Protein, SIGMA3. Cell(Cambridge,Mass.) V. 108 283 2002.
ISSN: ISSN 0092-8674
PubMed: 11832217
DOI: 10.1016/S0092-8674(02)00612-8