Atomistry » Manganese » PDB 1pj4-1r1o » 1qnm
Atomistry »
  Manganese »
    PDB 1pj4-1r1o »
      1qnm »

Manganese in PDB 1qnm: Human Manganese Superoxide Dismutase Mutant Q143N

Enzymatic activity of Human Manganese Superoxide Dismutase Mutant Q143N

All present enzymatic activity of Human Manganese Superoxide Dismutase Mutant Q143N:
1.15.1.1;

Protein crystallography data

The structure of Human Manganese Superoxide Dismutase Mutant Q143N, PDB code: 1qnm was solved by Y.Guan, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 2.30
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 75.500, 78.600, 67.700, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 28.7

Manganese Binding Sites:

The binding sites of Manganese atom in the Human Manganese Superoxide Dismutase Mutant Q143N (pdb code 1qnm). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Human Manganese Superoxide Dismutase Mutant Q143N, PDB code: 1qnm:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1qnm

Go back to Manganese Binding Sites List in 1qnm
Manganese binding site 1 out of 2 in the Human Manganese Superoxide Dismutase Mutant Q143N


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Human Manganese Superoxide Dismutase Mutant Q143N within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn199

b:30.1
occ:1.00
OD2 A:ASP159 1.9 23.6 1.0
NE2 A:HIS74 2.1 28.9 1.0
O A:HOH200 2.3 22.0 1.0
NE2 A:HIS26 2.3 37.2 1.0
NE2 A:HIS163 2.3 25.2 1.0
CE1 A:HIS74 2.8 29.3 1.0
CG A:ASP159 3.0 23.6 1.0
CD2 A:HIS163 3.2 28.3 1.0
CE1 A:HIS26 3.2 35.1 1.0
CD2 A:HIS26 3.3 37.2 1.0
CD2 A:HIS74 3.3 24.8 1.0
CE1 A:HIS163 3.4 25.8 1.0
OD1 A:ASP159 3.5 24.4 1.0
O A:HOH230 3.8 49.2 1.0
ND1 A:HIS74 4.0 26.5 1.0
CG A:HIS74 4.3 32.8 1.0
CB A:ASP159 4.3 24.1 1.0
CZ2 A:TRP123 4.3 26.5 1.0
ND1 A:HIS26 4.3 33.4 1.0
CG A:HIS163 4.4 30.0 1.0
ND1 A:HIS163 4.4 24.0 1.0
CG A:HIS26 4.4 35.4 1.0
CB A:TRP161 4.5 24.3 1.0
CG A:TRP161 4.6 25.7 1.0
CH2 A:TRP123 4.9 17.1 1.0
CD1 A:TRP161 4.9 22.9 1.0
CE2 A:TRP123 5.0 23.8 1.0

Manganese binding site 2 out of 2 in 1qnm

Go back to Manganese Binding Sites List in 1qnm
Manganese binding site 2 out of 2 in the Human Manganese Superoxide Dismutase Mutant Q143N


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Human Manganese Superoxide Dismutase Mutant Q143N within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn199

b:32.8
occ:1.00
OD2 B:ASP159 2.1 34.3 1.0
NE2 B:HIS163 2.1 27.3 1.0
NE2 B:HIS26 2.1 36.0 1.0
O B:HOH200 2.1 26.8 1.0
NE2 B:HIS74 2.2 33.6 1.0
CE1 B:HIS74 2.9 34.5 1.0
CE1 B:HIS26 3.0 34.5 1.0
CE1 B:HIS163 3.1 22.1 1.0
CD2 B:HIS163 3.1 34.5 1.0
CD2 B:HIS26 3.1 36.4 1.0
CG B:ASP159 3.2 25.9 1.0
CD2 B:HIS74 3.3 36.0 1.0
OD1 B:ASP159 3.6 23.4 1.0
O B:HOH215 3.8 33.9 1.0
ND1 B:HIS74 4.1 34.5 1.0
ND1 B:HIS26 4.2 35.8 1.0
ND1 B:HIS163 4.2 26.9 1.0
CG B:HIS163 4.2 38.5 1.0
CG B:HIS26 4.3 37.6 1.0
CG B:HIS74 4.4 35.8 1.0
CZ2 B:TRP123 4.4 19.7 1.0
CB B:ASP159 4.5 27.5 1.0
CG B:TRP161 4.7 23.0 1.0
CB B:TRP161 4.7 27.5 1.0
CB B:ALA164 4.8 30.1 1.0
CD1 B:TRP161 4.9 27.2 1.0
CH2 B:TRP123 4.9 21.5 1.0
CD2 B:TRP161 5.0 22.0 1.0

Reference:

Y.Hsieh, Y.Guan, C.Tu, P.J.Bratt, A.Angerhofer, J.R.Lepock, M.J.Hickey, J.A.Tainer, H.S.Nick, D.N.Silverman. Probing the Active Site of Human Manganese Superoxide Dismutase: the Role of Glutamine 143. Biochemistry V. 37 4731 1998.
ISSN: ISSN 0006-2960
PubMed: 9537988
DOI: 10.1021/BI972395D
Page generated: Tue Dec 15 03:54:48 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy