Manganese in PDB 1em1: X-Ray Crystal Structure For Human Manganese Superoxide Dismutase, Q143A

All present enzymatic activity of X-Ray Crystal Structure For Human Manganese Superoxide Dismutase, Q143A:
1.15.1.1;

The structure of X-Ray Crystal Structure For Human Manganese Superoxide Dismutase, Q143A, PDB code: 1em1 was solved by V.Leveque, M.E.Stroupe, J.R.Lepock, D.E.Cabelli, J.A.Tainer, H.S.Nick, D.N.Silverman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.79 / 2.13
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	79.643, 79.643, 241.642, 90.00, 90.00, 120.00
R / Rfree (%)	23.2 / 26.4

The binding sites of Manganese atom in the X-Ray Crystal Structure For Human Manganese Superoxide Dismutase, Q143A (pdb code 1em1). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the X-Ray Crystal Structure For Human Manganese Superoxide Dismutase, Q143A, PDB code: 1em1:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the X-Ray Crystal Structure For Human Manganese Superoxide Dismutase, Q143A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of X-Ray Crystal Structure For Human Manganese Superoxide Dismutase, Q143A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn600 b:20.6 occ:1.00 NE2 A:HIS163 2.1 20.4 1.0 NE2 A:HIS74 2.1 20.2 1.0 NE2 A:HIS26 2.1 21.6 1.0 OD1 A:ASP159 2.1 20.0 1.0 O A:HOH763 2.2 20.0 1.0 CE1 A:HIS74 3.0 20.2 1.0 CE1 A:HIS26 3.0 21.8 1.0 CE1 A:HIS163 3.1 20.5 1.0 CD2 A:HIS163 3.1 20.5 1.0 CD2 A:HIS74 3.2 20.1 1.0 CD2 A:HIS26 3.2 21.8 1.0 CG A:ASP159 3.2 19.8 1.0 OD2 A:ASP159 3.6 19.7 1.0 ND1 A:HIS74 4.2 20.1 1.0 CZ2 A:TRP123 4.2 19.6 1.0 ND1 A:HIS163 4.2 20.3 1.0 ND1 A:HIS26 4.2 21.9 1.0 CG A:HIS163 4.2 20.5 1.0 CG A:HIS74 4.3 20.1 1.0 CG A:HIS26 4.3 22.1 1.0 O A:HOH696 4.4 41.8 1.0 CB A:ASP159 4.5 19.8 1.0 CB A:TRP161 4.6 19.8 1.0 CG A:TRP161 4.7 19.8 1.0 CH2 A:TRP123 4.8 19.6 1.0 CE2 A:TRP123 4.9 19.7 1.0 CB A:ALA164 4.9 21.1 1.0 CD1 A:TRP161 5.0 19.7 1.0

Manganese binding site 2 out of 2 in the X-Ray Crystal Structure For Human Manganese Superoxide Dismutase, Q143A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of X-Ray Crystal Structure For Human Manganese Superoxide Dismutase, Q143A within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn601 b:18.4 occ:1.00 OD1 B:ASP159 2.0 19.0 1.0 NE2 B:HIS163 2.2 19.0 1.0 NE2 B:HIS26 2.2 18.8 1.0 NE2 B:HIS74 2.3 18.8 1.0 O B:HOH731 2.3 17.9 1.0 CE1 B:HIS163 3.1 19.1 1.0 CG B:ASP159 3.1 19.3 1.0 CE1 B:HIS26 3.2 18.9 1.0 CD2 B:HIS26 3.2 18.9 1.0 CE1 B:HIS74 3.2 18.9 1.0 CD2 B:HIS74 3.2 18.9 1.0 CD2 B:HIS163 3.3 19.1 1.0 OD2 B:ASP159 3.6 19.3 1.0 CZ2 B:TRP123 4.2 22.4 1.0 ND1 B:HIS163 4.3 19.1 1.0 ND1 B:HIS26 4.3 19.0 1.0 CG B:HIS26 4.3 19.1 1.0 ND1 B:HIS74 4.3 18.9 1.0 CG B:HIS163 4.4 19.1 1.0 CG B:HIS74 4.4 19.0 1.0 CB B:ASP159 4.4 19.2 1.0 CB B:TRP161 4.6 18.1 1.0 O B:HOH695 4.8 49.8 1.0 CG B:TRP161 4.8 18.1 1.0 CB B:ALA164 4.8 19.4 1.0 CH2 B:TRP123 4.8 22.4 1.0 CE2 B:TRP123 4.9 22.5 1.0 CD1 B:TRP161 5.0 18.0 1.0

V.J.Leveque, M.E.Stroupe, J.R.Lepock, D.E.Cabelli, J.A.Tainer, H.S.Nick, D.N.Silverman. Multiple Replacements of Glutamine 143 in Human Manganese Superoxide Dismutase: Effects on Structure, Stability, and Catalysis. Biochemistry V. 39 7131 2000.
ISSN: ISSN 0006-2960
PubMed: 10852710
DOI: 10.1021/BI9929958