Atomistry » Manganese » PDB 1pj4-1r1o » 1pm9
Atomistry »
  Manganese »
    PDB 1pj4-1r1o »
      1pm9 »

Manganese in PDB 1pm9: Crystal Structure of Human Mnsod H30N, Y166F Mutant

Enzymatic activity of Crystal Structure of Human Mnsod H30N, Y166F Mutant

All present enzymatic activity of Crystal Structure of Human Mnsod H30N, Y166F Mutant:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Mnsod H30N, Y166F Mutant, PDB code: 1pm9 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 / 1.70
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 71.580, 76.460, 66.610, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 23.9

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Human Mnsod H30N, Y166F Mutant (pdb code 1pm9). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Human Mnsod H30N, Y166F Mutant, PDB code: 1pm9:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1pm9

Go back to Manganese Binding Sites List in 1pm9
Manganese binding site 1 out of 2 in the Crystal Structure of Human Mnsod H30N, 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 H30N, Y166F Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn200

b:11.5
occ:1.00
OD2 A:ASP159 2.0 12.2 1.0
O A:HOH201 2.0 9.0 1.0
NE2 A:HIS26 2.1 7.7 1.0
NE2 A:HIS74 2.1 11.4 1.0
NE2 A:HIS163 2.2 12.4 1.0
CE1 A:HIS74 3.0 7.4 1.0
CE1 A:HIS26 3.0 9.9 1.0
CG A:ASP159 3.1 11.4 1.0
CE1 A:HIS163 3.1 10.1 1.0
CD2 A:HIS26 3.1 11.1 1.0
CD2 A:HIS74 3.2 7.7 1.0
CD2 A:HIS163 3.2 11.7 1.0
OD1 A:ASN30 3.4 22.0 1.0
OD1 A:ASP159 3.5 12.2 1.0
CZ2 A:TRP123 4.2 11.1 1.0
ND1 A:HIS74 4.2 8.2 1.0
ND1 A:HIS26 4.2 11.6 1.0
ND1 A:HIS163 4.3 11.8 1.0
CG A:HIS26 4.3 8.9 1.0
CG A:HIS74 4.3 8.2 1.0
CB A:ASP159 4.3 10.6 1.0
CG A:HIS163 4.3 12.0 1.0
NE2 A:GLN143 4.4 9.6 1.0
CG A:ASN30 4.4 21.0 1.0
CB A:TRP161 4.5 10.6 1.0
CG A:TRP161 4.6 9.5 1.0
CH2 A:TRP123 4.8 9.4 1.0
CD1 A:TRP161 4.9 9.6 1.0
CE2 A:TRP123 4.9 10.0 1.0
CB A:ALA164 5.0 9.5 1.0

Manganese binding site 2 out of 2 in 1pm9

Go back to Manganese Binding Sites List in 1pm9
Manganese binding site 2 out of 2 in the Crystal Structure of Human Mnsod H30N, 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 H30N, Y166F Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn200

b:14.3
occ:1.00
OD2 B:ASP159 2.0 11.4 1.0
O B:HOH202 2.0 12.3 1.0
NE2 B:HIS26 2.1 10.2 1.0
NE2 B:HIS74 2.1 10.7 1.0
NE2 B:HIS163 2.2 12.9 1.0
CE1 B:HIS26 3.1 12.0 1.0
CE1 B:HIS74 3.1 9.6 1.0
CG B:ASP159 3.1 11.5 1.0
CE1 B:HIS163 3.1 10.2 1.0
CD2 B:HIS26 3.1 10.1 1.0
OD1 B:ASN30 3.1 26.0 1.0
CD2 B:HIS74 3.2 10.3 1.0
CD2 B:HIS163 3.2 11.0 1.0
OD1 B:ASP159 3.5 11.3 1.0
ND1 B:HIS26 4.2 10.2 1.0
CZ2 B:TRP123 4.2 11.9 1.0
ND1 B:HIS74 4.2 9.7 1.0
ND1 B:HIS163 4.2 11.4 1.0
CG B:HIS26 4.2 11.6 1.0
CG B:HIS74 4.3 10.2 1.0
CG B:ASN30 4.3 25.6 1.0
CG B:HIS163 4.3 11.3 1.0
CB B:ASP159 4.3 11.3 1.0
NE2 B:GLN143 4.4 13.1 1.0
CB B:TRP161 4.5 11.1 1.0
CG B:TRP161 4.6 12.1 1.0
CH2 B:TRP123 4.8 11.6 1.0
CD1 B:TRP161 4.9 12.0 1.0
CE2 B:TRP123 4.9 10.9 1.0
CB B:ALA164 4.9 13.0 1.0

Reference:

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
Page generated: Sat Oct 5 12:07:35 2024

Last articles

W in 8QLN
W in 8RJA
V in 8WTN
Te in 8QLN
Re in 9GHX
Rb in 8Z5C
Ni in 9C0T
Ni in 9C0S
Ni in 9GP1
Ni in 9FYO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy