Manganese in PDB 1pl4: Crystal Structure of Human Mnsod Y166F Mutant

All present enzymatic activity of Crystal Structure of Human Mnsod Y166F Mutant:
1.15.1.1;

The structure of Crystal Structure of Human Mnsod Y166F Mutant, PDB code: 1pl4 was solved by L.Fan, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.47
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.689, 77.711, 135.795, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 23.7

The binding sites of Manganese atom in the Crystal Structure of Human Mnsod Y166F Mutant (pdb code 1pl4). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Human Mnsod Y166F Mutant, PDB code: 1pl4:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of Human Mnsod Y166F Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Human Mnsod Y166F Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn200 b:11.0 occ:1.00 O A:HOH201 2.0 13.0 1.0 OD2 A:ASP159 2.1 14.4 1.0 NE2 A:HIS163 2.2 11.1 1.0 NE2 A:HIS26 2.2 14.6 1.0 NE2 A:HIS74 2.2 11.6 1.0 CG A:ASP159 3.1 14.0 1.0 CE1 A:HIS163 3.1 15.0 1.0 CE1 A:HIS26 3.1 11.3 1.0 CD2 A:HIS163 3.2 8.4 1.0 CD2 A:HIS26 3.2 15.1 1.0 CE1 A:HIS74 3.2 9.8 1.0 CD2 A:HIS74 3.2 11.8 1.0 OD1 A:ASP159 3.5 12.8 1.0 CD2 A:HIS30 4.1 23.8 1.0 CZ2 A:TRP123 4.2 10.8 1.0 ND1 A:HIS163 4.2 12.8 1.0 ND1 A:HIS26 4.3 11.8 1.0 ND1 A:HIS74 4.3 9.0 1.0 CG A:HIS163 4.3 8.6 1.0 CG A:HIS26 4.3 12.9 1.0 CG A:HIS74 4.4 8.8 1.0 NE2 A:GLN143 4.4 12.6 1.0 CB A:ASP159 4.4 12.3 1.0 NE2 A:HIS30 4.5 23.8 1.0 CB A:TRP161 4.6 9.8 1.0 CG A:TRP161 4.6 11.2 1.0 CH2 A:TRP123 4.8 9.8 1.0 CD1 A:TRP161 4.8 12.1 1.0 CE2 A:TRP123 5.0 11.9 1.0 CG A:HIS30 5.0 27.2 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Human Mnsod Y166F Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Human Mnsod Y166F Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn200 b:10.4 occ:1.00 OD2 B:ASP159 2.0 13.7 1.0 O B:HOH202 2.1 16.7 1.0 NE2 B:HIS74 2.1 12.2 1.0 NE2 B:HIS26 2.2 14.7 1.0 NE2 B:HIS163 2.2 11.5 1.0 CG B:ASP159 3.0 14.1 1.0 CE1 B:HIS74 3.1 12.2 1.0 CE1 B:HIS26 3.1 10.9 1.0 CE1 B:HIS163 3.1 13.1 1.0 CD2 B:HIS74 3.2 11.8 1.0 CD2 B:HIS163 3.2 11.6 1.0 CD2 B:HIS26 3.3 11.2 1.0 OD1 B:ASP159 3.4 16.7 1.0 ND1 B:HIS74 4.2 13.8 1.0 CZ2 B:TRP123 4.2 13.8 1.0 ND1 B:HIS26 4.2 13.9 1.0 ND1 B:HIS163 4.3 13.6 1.0 CG B:HIS74 4.3 10.7 1.0 CB B:ASP159 4.3 9.4 1.0 CG B:HIS26 4.3 13.6 1.0 CG B:HIS163 4.4 13.0 1.0 CD2 B:HIS30 4.4 27.5 1.0 NE2 B:GLN143 4.4 9.2 1.0 CB B:TRP161 4.6 9.7 1.0 CG B:TRP161 4.6 12.5 1.0 NE2 B:HIS30 4.8 19.9 1.0 CH2 B:TRP123 4.8 13.2 1.0 CD1 B:TRP161 4.8 10.4 1.0 CE2 B:TRP123 5.0 12.5 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Human Mnsod Y166F Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Human Mnsod Y166F Mutant within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn200 b:10.4 occ:1.00 O C:HOH203 2.0 14.3 1.0 OD2 C:ASP159 2.0 13.1 1.0 NE2 C:HIS163 2.2 11.6 1.0 NE2 C:HIS26 2.2 12.7 1.0 NE2 C:HIS74 2.2 13.7 1.0 CG C:ASP159 3.1 15.8 1.0 CE1 C:HIS26 3.1 11.0 1.0 CE1 C:HIS74 3.2 12.2 1.0 CD2 C:HIS163 3.2 15.6 1.0 CE1 C:HIS163 3.2 13.4 1.0 CD2 C:HIS74 3.2 16.2 1.0 CD2 C:HIS26 3.2 12.3 1.0 OD1 C:ASP159 3.5 13.0 1.0 ND1 C:HIS26 4.2 11.7 1.0 CZ2 C:TRP123 4.2 11.0 1.0 ND1 C:HIS74 4.3 11.8 1.0 ND1 C:HIS163 4.3 14.0 1.0 CG C:HIS26 4.3 12.3 1.0 CG C:HIS74 4.3 13.1 1.0 CG C:HIS163 4.3 12.7 1.0 CB C:ASP159 4.4 9.6 1.0 NE2 C:GLN143 4.4 11.3 1.0 CD2 C:HIS30 4.5 36.8 1.0 CB C:TRP161 4.6 9.5 1.0 CG C:TRP161 4.6 8.0 1.0 CD1 C:TRP161 4.8 11.5 1.0 CH2 C:TRP123 4.9 14.1 1.0 NE2 C:HIS30 4.9 32.9 1.0 CE2 C:TRP123 5.0 10.4 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Human Mnsod Y166F Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Human Mnsod Y166F Mutant within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn200 b:10.0 occ:1.00 O D:HOH204 1.9 10.6 1.0 OD2 D:ASP159 2.0 10.0 1.0 NE2 D:HIS74 2.1 9.1 1.0 NE2 D:HIS26 2.2 9.1 1.0 NE2 D:HIS163 2.2 9.9 1.0 CG D:ASP159 3.0 9.8 1.0 CE1 D:HIS26 3.1 12.6 1.0 CE1 D:HIS74 3.1 9.6 1.0 CE1 D:HIS163 3.1 7.4 1.0 CD2 D:HIS163 3.2 11.9 1.0 CD2 D:HIS74 3.2 9.1 1.0 CD2 D:HIS26 3.2 9.2 1.0 OD1 D:ASP159 3.4 12.3 1.0 CD2 D:HIS30 4.2 21.4 1.0 ND1 D:HIS74 4.2 11.3 1.0 ND1 D:HIS26 4.2 11.6 1.0 ND1 D:HIS163 4.2 9.2 1.0 CZ2 D:TRP123 4.2 9.8 1.0 CG D:HIS74 4.3 7.8 1.0 CB D:ASP159 4.3 8.9 1.0 CG D:HIS26 4.3 10.4 1.0 CG D:HIS163 4.3 10.4 1.0 NE2 D:GLN143 4.5 12.1 1.0 NE2 D:HIS30 4.5 14.1 1.0 CB D:TRP161 4.6 8.0 1.0 CG D:TRP161 4.7 6.4 1.0 CH2 D:TRP123 4.8 12.4 1.0 CB D:ALA164 4.9 11.5 1.0 CD1 D:TRP161 4.9 11.8 1.0 CE2 D:TRP123 5.0 11.9 1.0

A.S.Hearn, L.Fan, J.R.Lepock, J.P.Luba, W.B.Greenleaf, D.E.Cabelli, J.A.Tainer, H.S.Nick, D.N.Silverman. Amino Acid Substitution at the Dimeric Interface of Human Manganese Superoxide Dismutase J.Biol.Chem. V. 279 5861 2004.
ISSN: ISSN 0021-9258
PubMed: 14638684
DOI: 10.1074/JBC.M311310200