Atomistry » Iron » PDB 3ebd-3esf » 3esf
Atomistry »
  Iron »
    PDB 3ebd-3esf »
      3esf »

Iron in PDB 3esf: Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei

Enzymatic activity of Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei

All present enzymatic activity of Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei, PDB code: 3esf was solved by J.F.R.Bachega, M.V.A.S.Navarro, R.C.Garratt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.18 / 2.01
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 68.302, 76.504, 76.981, 90.00, 92.70, 90.00
R / Rfree (%) 17.5 / 21.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei (pdb code 3esf). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei, PDB code: 3esf:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3esf

Go back to Iron Binding Sites List in 3esf
Iron binding site 1 out of 4 in the Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe198

b:21.7
occ:1.00
OD2 A:ASP161 2.0 22.6 1.0
NE2 A:HIS165 2.1 20.9 1.0
O A:HOH199 2.1 20.3 1.0
NE2 A:HIS76 2.2 18.7 1.0
NE2 A:HIS28 2.2 15.7 1.0
CD2 A:HIS165 3.0 19.5 1.0
CD2 A:HIS76 3.1 19.1 1.0
CE1 A:HIS76 3.1 20.7 1.0
CG A:ASP161 3.1 21.3 1.0
CE1 A:HIS28 3.1 16.4 1.0
CE1 A:HIS165 3.2 18.3 1.0
CD2 A:HIS28 3.2 16.1 1.0
OD1 A:ASP161 3.6 18.6 1.0
CG A:HIS165 4.2 18.4 1.0
ND1 A:HIS76 4.2 17.8 1.0
ND1 A:HIS165 4.2 18.6 1.0
CG A:HIS76 4.2 19.2 1.0
ND1 A:HIS28 4.2 16.5 1.0
CG A:HIS28 4.3 17.2 1.0
CB A:ASP161 4.4 19.9 1.0
CH2 A:TRP125 4.5 18.1 1.0
CB A:TRP163 4.6 18.5 1.0
CZ2 A:TRP125 4.6 17.9 1.0
CG A:TRP163 4.8 19.6 1.0
CB A:ALA166 4.8 18.7 1.0
CB A:HIS32 4.9 19.7 1.0
NE2 A:GLN72 5.0 20.4 1.0

Iron binding site 2 out of 4 in 3esf

Go back to Iron Binding Sites List in 3esf
Iron binding site 2 out of 4 in the Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe198

b:23.9
occ:1.00
OD2 B:ASP161 2.0 22.2 1.0
NE2 B:HIS76 2.1 23.0 1.0
NE2 B:HIS165 2.1 19.5 1.0
NE2 B:HIS28 2.3 16.9 1.0
O B:HOH200 2.3 19.0 1.0
CE1 B:HIS76 3.0 20.1 1.0
CD2 B:HIS76 3.0 20.7 1.0
CD2 B:HIS165 3.0 18.9 1.0
CG B:ASP161 3.1 21.1 1.0
CE1 B:HIS165 3.1 17.9 1.0
CD2 B:HIS28 3.2 17.1 1.0
CE1 B:HIS28 3.2 18.3 1.0
OD1 B:ASP161 3.5 20.3 1.0
ND1 B:HIS76 4.1 19.2 1.0
CG B:HIS76 4.1 21.3 1.0
CG B:HIS165 4.2 18.4 1.0
ND1 B:HIS165 4.2 19.5 1.0
ND1 B:HIS28 4.3 16.9 1.0
CG B:HIS28 4.3 17.5 1.0
CB B:ASP161 4.4 20.5 1.0
CB B:TRP163 4.4 18.4 1.0
CH2 B:TRP125 4.5 17.7 1.0
CZ2 B:TRP125 4.6 19.6 1.0
CB B:ALA166 4.6 18.9 1.0
CG B:TRP163 4.7 19.4 1.0
N B:ALA166 5.0 19.6 1.0

Iron binding site 3 out of 4 in 3esf

Go back to Iron Binding Sites List in 3esf
Iron binding site 3 out of 4 in the Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe198

b:24.2
occ:1.00
OD2 C:ASP161 2.0 21.6 1.0
NE2 C:HIS165 2.1 19.4 1.0
NE2 C:HIS76 2.1 19.6 1.0
NE2 C:HIS28 2.2 17.5 1.0
O C:HOH201 2.3 21.5 1.0
CD2 C:HIS165 3.0 17.9 1.0
CE1 C:HIS76 3.1 19.4 1.0
CD2 C:HIS76 3.1 18.7 1.0
CE1 C:HIS165 3.1 16.0 1.0
CE1 C:HIS28 3.1 16.4 1.0
CG C:ASP161 3.2 21.1 1.0
CD2 C:HIS28 3.2 15.3 1.0
OD1 C:ASP161 3.6 18.3 1.0
CG C:HIS165 4.2 17.9 1.0
ND1 C:HIS76 4.2 17.2 1.0
ND1 C:HIS165 4.2 19.1 1.0
CG C:HIS76 4.2 19.9 1.0
ND1 C:HIS28 4.2 17.4 1.0
CG C:HIS28 4.3 17.3 1.0
CB C:ASP161 4.4 20.1 1.0
CH2 C:TRP125 4.5 18.0 1.0
CB C:TRP163 4.5 19.2 1.0
CZ2 C:TRP125 4.6 18.3 1.0
CG C:TRP163 4.7 19.4 1.0
CB C:ALA166 4.8 18.6 1.0
CB C:HIS32 4.9 19.2 1.0

Iron binding site 4 out of 4 in 3esf

Go back to Iron Binding Sites List in 3esf
Iron binding site 4 out of 4 in the Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of the Enzyme Fe-Superoxide Dismutase TBSODB2 From Trypanosoma Brucei within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe198

b:23.4
occ:1.00
OD2 D:ASP161 2.0 20.9 1.0
NE2 D:HIS76 2.1 19.1 1.0
NE2 D:HIS165 2.2 21.2 1.0
NE2 D:HIS28 2.2 17.5 1.0
O D:HOH202 2.2 27.6 1.0
CD2 D:HIS76 3.0 18.8 1.0
CD2 D:HIS165 3.0 19.3 1.0
CE1 D:HIS76 3.1 18.4 1.0
CE1 D:HIS28 3.1 16.9 1.0
CG D:ASP161 3.1 20.6 1.0
CD2 D:HIS28 3.2 14.4 1.0
CE1 D:HIS165 3.3 18.9 1.0
OD1 D:ASP161 3.6 19.0 1.0
CG D:HIS76 4.2 18.8 1.0
ND1 D:HIS76 4.2 18.2 1.0
CG D:HIS165 4.2 18.0 1.0
ND1 D:HIS28 4.2 16.4 1.0
CG D:HIS28 4.3 17.1 1.0
ND1 D:HIS165 4.3 18.4 1.0
CH2 D:TRP125 4.3 18.0 1.0
CB D:ASP161 4.4 19.8 1.0
CB D:TRP163 4.6 18.4 1.0
CZ2 D:TRP125 4.6 18.9 1.0
CG D:TRP163 4.8 18.1 1.0
CB D:ALA166 4.8 18.1 1.0
CB D:HIS32 5.0 19.2 1.0

Reference:

J.F.Bachega, M.V.Navarro, L.Bleicher, R.K.Bortoleto-Bugs, D.Dive, P.Hoffmann, E.Viscogliosi, R.C.Garratt. Systematic Structural Studies of Iron Superoxide Dismutases From Human Parasites and A Statistical Coupling Analysis of Metal Binding Specificity Proteins V. 77 26 2009.
ISSN: ISSN 0887-3585
PubMed: 19384994
DOI: 10.1002/PROT.22412
Page generated: Sun Dec 13 15:05:16 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