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Iron in PDB 1mmm: Distinct Metal Environment in Iron-Substituted Manganese Superoxide Dismutase Provides A Structural Basis of Metal Specificity

Enzymatic activity of Distinct Metal Environment in Iron-Substituted Manganese Superoxide Dismutase Provides A Structural Basis of Metal Specificity

All present enzymatic activity of Distinct Metal Environment in Iron-Substituted Manganese Superoxide Dismutase Provides A Structural Basis of Metal Specificity:
1.15.1.1;

Protein crystallography data

The structure of Distinct Metal Environment in Iron-Substituted Manganese Superoxide Dismutase Provides A Structural Basis of Metal Specificity, PDB code: 1mmm was solved by R.A.Edwards, M.M.Whittaker, J.W.Whittaker, G.B.Jameson, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 46.190, 89.040, 206.671, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 23.1

Iron Binding Sites:

The binding sites of Iron atom in the Distinct Metal Environment in Iron-Substituted Manganese Superoxide Dismutase Provides A Structural Basis of Metal Specificity (pdb code 1mmm). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Distinct Metal Environment in Iron-Substituted Manganese Superoxide Dismutase Provides A Structural Basis of Metal Specificity, PDB code: 1mmm:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1mmm

Go back to Iron Binding Sites List in 1mmm
Iron binding site 1 out of 2 in the Distinct Metal Environment in Iron-Substituted Manganese Superoxide Dismutase Provides A Structural Basis of Metal Specificity


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Distinct Metal Environment in Iron-Substituted Manganese Superoxide Dismutase Provides A Structural Basis of Metal Specificity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe206

b:12.3
occ:1.00
NE2 A:HIS81 2.1 6.7 1.0
OD2 A:ASP167 2.1 11.1 1.0
NE2 A:HIS26 2.2 3.7 1.0
O A:OH207 2.2 6.6 1.0
NE2 A:HIS171 2.3 8.3 1.0
CE1 A:HIS81 2.9 8.8 1.0
CE1 A:HIS26 3.1 4.4 1.0
CD2 A:HIS81 3.1 5.3 1.0
CE1 A:HIS171 3.2 7.5 1.0
CD2 A:HIS26 3.2 2.4 1.0
CG A:ASP167 3.2 10.2 1.0
CD2 A:HIS171 3.3 8.7 1.0
OD1 A:ASP167 3.6 9.8 1.0
ND1 A:HIS81 4.1 7.6 1.0
CG A:HIS81 4.2 5.7 1.0
ND1 A:HIS26 4.2 3.8 1.0
CG A:HIS26 4.3 4.2 1.0
ND1 A:HIS171 4.3 9.3 1.0
CB A:ASP167 4.4 7.6 1.0
NE2 A:GLN146 4.4 8.9 1.0
CZ2 A:TRP128 4.4 5.8 1.0
CG A:HIS171 4.4 9.0 1.0
OH A:TYR34 4.4 18.4 1.0
CB A:TRP169 4.7 5.2 1.0
CG A:TRP169 4.8 6.2 1.0
CE2 A:TYR34 4.9 15.6 1.0
CH2 A:TRP128 4.9 7.4 1.0
CB A:ALA172 5.0 4.1 1.0

Iron binding site 2 out of 2 in 1mmm

Go back to Iron Binding Sites List in 1mmm
Iron binding site 2 out of 2 in the Distinct Metal Environment in Iron-Substituted Manganese Superoxide Dismutase Provides A Structural Basis of Metal Specificity


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Distinct Metal Environment in Iron-Substituted Manganese Superoxide Dismutase Provides A Structural Basis of Metal Specificity within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe206

b:13.9
occ:1.00
O B:OH208 2.0 19.4 1.0
OD2 B:ASP167 2.0 7.0 1.0
NE2 B:HIS81 2.2 8.5 1.0
NE2 B:HIS26 2.2 6.5 1.0
O B:OH207 2.2 5.1 1.0
NE2 B:HIS171 2.3 8.2 1.0
CG B:ASP167 3.0 8.7 1.0
CE1 B:HIS26 3.1 6.4 1.0
CD2 B:HIS81 3.2 9.4 1.0
CE1 B:HIS81 3.2 10.6 1.0
CE1 B:HIS171 3.2 7.8 1.0
CD2 B:HIS26 3.3 7.1 1.0
CD2 B:HIS171 3.4 8.7 1.0
OD1 B:ASP167 3.5 11.3 1.0
ND1 B:HIS26 4.2 5.2 1.0
CB B:ASP167 4.2 7.3 1.0
ND1 B:HIS81 4.3 9.6 1.0
CG B:HIS81 4.3 10.8 1.0
ND1 B:HIS171 4.4 5.8 1.0
CG B:HIS26 4.4 6.9 1.0
OH B:TYR34 4.4 13.7 1.0
CG B:HIS171 4.5 7.1 1.0
NE2 B:GLN146 4.5 6.2 1.0
CZ2 B:TRP128 4.6 7.1 1.0
CB B:TRP169 4.7 6.5 1.0
CG B:TRP169 4.8 8.2 1.0
CB B:ALA172 5.0 5.4 1.0
CE2 B:TYR34 5.0 12.5 1.0

Reference:

R.A.Edwards, M.M.Whittaker, J.W.Whittaker, G.B.Jameson, E.N.Baker. Distinct Metal Environment in Fe-Substituted Manganese Superoxide Dismutase Provides A Structural Basis of Metal Specificity J.Am.Chem.Soc. V. 120 9684 1998.
ISSN: ISSN 0002-7863
Page generated: Sun Dec 13 14:24:06 2020

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