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Iron in PDB 4tog: 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa

Enzymatic activity of 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa

All present enzymatic activity of 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa:
1.16.3.1;

Protein crystallography data

The structure of 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa, PDB code: 4tog was solved by S.Lovell, K.P.Battaile, H.Yao, R.Kumar, K.Eshelman, M.Rivera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.27 / 1.80
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 155.134, 155.134, 155.177, 90.00, 90.00, 120.00
R / Rfree (%) 15.3 / 17.8

Other elements in 4tog:

The structure of 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa also contains other interesting chemical elements:

Potassium (K) 1 atom
Sodium (Na) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa (pdb code 4tog). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa, PDB code: 4tog:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4tog

Go back to Iron Binding Sites List in 4tog
Iron binding site 1 out of 4 in the 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:22.2
occ:0.50
 FE A:HEM201 0.0 22.2 0.5
FE A:HEM201 0.3 22.3 0.5
ND A:HEM201 1.9 21.7 0.5
NA A:HEM201 2.0 21.7 0.5
NC A:HEM201 2.0 19.2 0.5
NB A:HEM201 2.0 19.4 0.5
ND A:HEM201 2.1 20.6 0.5
NA A:HEM201 2.1 20.5 0.5
NC A:HEM201 2.1 22.2 0.5
NB A:HEM201 2.2 22.0 0.5
SD A:MET52 2.4 20.7 1.0
SD B:MET52 2.4 19.9 1.0
C1D A:HEM201 2.9 23.7 0.5
C4C A:HEM201 2.9 22.4 0.5
C4D A:HEM201 3.0 23.6 0.5
C1A A:HEM201 3.0 23.5 0.5
C4A A:HEM201 3.0 23.3 0.5
C4D A:HEM201 3.0 23.2 0.5
C1A A:HEM201 3.0 23.1 0.5
C1B A:HEM201 3.0 22.3 0.5
C1C A:HEM201 3.1 22.2 0.5
C4B A:HEM201 3.1 22.5 0.5
C1C A:HEM201 3.1 23.1 0.5
C1D A:HEM201 3.2 22.2 0.5
C4C A:HEM201 3.2 23.3 0.5
C4A A:HEM201 3.2 22.5 0.5
C4B A:HEM201 3.2 23.3 0.5
CHD A:HEM201 3.3 23.9 0.5
CE A:MET52 3.3 21.9 1.0
C1B A:HEM201 3.3 23.9 0.5
CHA A:HEM201 3.3 21.0 0.5
CHA A:HEM201 3.3 21.0 0.5
CE B:MET52 3.4 19.2 1.0
CHB A:HEM201 3.4 23.9 0.5
CHC A:HEM201 3.4 23.3 0.5
CHC A:HEM201 3.5 22.9 0.5
CG B:MET52 3.5 18.6 1.0
CHD A:HEM201 3.6 22.8 0.5
CG A:MET52 3.6 18.9 1.0
CHB A:HEM201 3.7 21.3 0.5
C2D A:HEM201 4.1 21.4 0.5
C3D A:HEM201 4.2 23.6 0.5
C2A A:HEM201 4.2 23.5 0.5
C3A A:HEM201 4.2 20.6 0.5
C3C A:HEM201 4.2 22.8 0.5
C2C A:HEM201 4.2 20.1 0.5
CB B:MET52 4.3 17.9 1.0
C2B A:HEM201 4.3 22.6 0.5
C2A A:HEM201 4.3 21.5 0.5
C3D A:HEM201 4.3 21.2 0.5
C3B A:HEM201 4.3 19.8 0.5
CB A:MET52 4.3 18.4 1.0
C2C A:HEM201 4.4 21.4 0.5
C2D A:HEM201 4.4 20.5 0.5
C3A A:HEM201 4.4 20.7 0.5
C3C A:HEM201 4.4 23.6 0.5
C3B A:HEM201 4.5 23.6 0.5
C2B A:HEM201 4.5 21.8 0.5

Iron binding site 2 out of 4 in 4tog

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Iron binding site 2 out of 4 in the 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:22.3
occ:0.50
 FE A:HEM201 0.0 22.3 0.5
FE A:HEM201 0.3 22.2 0.5
NC A:HEM201 1.9 22.2 0.5
NB A:HEM201 2.0 22.0 0.5
ND A:HEM201 2.0 20.6 0.5
NA A:HEM201 2.0 20.5 0.5
NC A:HEM201 2.0 19.2 0.5
NB A:HEM201 2.1 19.4 0.5
ND A:HEM201 2.2 21.7 0.5
NA A:HEM201 2.2 21.7 0.5
SD B:MET52 2.3 19.9 1.0
SD A:MET52 2.4 20.7 1.0
C1C A:HEM201 2.9 23.1 0.5
C4C A:HEM201 2.9 23.3 0.5
C1D A:HEM201 3.0 22.2 0.5
C4B A:HEM201 3.0 23.3 0.5
C1C A:HEM201 3.0 22.2 0.5
C1B A:HEM201 3.0 23.9 0.5
C4D A:HEM201 3.0 23.2 0.5
C4A A:HEM201 3.0 22.5 0.5
C1A A:HEM201 3.0 23.1 0.5
C4B A:HEM201 3.1 22.5 0.5
C4C A:HEM201 3.1 22.4 0.5
C4D A:HEM201 3.2 23.6 0.5
C1A A:HEM201 3.2 23.5 0.5
C1D A:HEM201 3.2 23.7 0.5
CE B:MET52 3.2 19.2 1.0
C1B A:HEM201 3.2 22.3 0.5
C4A A:HEM201 3.3 23.3 0.5
CHD A:HEM201 3.3 22.8 0.5
CHC A:HEM201 3.3 23.3 0.5
CHC A:HEM201 3.4 22.9 0.5
CHB A:HEM201 3.4 21.3 0.5
CE A:MET52 3.4 21.9 1.0
CHA A:HEM201 3.5 21.0 0.5
CHA A:HEM201 3.5 21.0 0.5
CHD A:HEM201 3.5 23.9 0.5
CG B:MET52 3.5 18.6 1.0
CG A:MET52 3.5 18.9 1.0
CHB A:HEM201 3.6 23.9 0.5
C2C A:HEM201 4.1 21.4 0.5
C3C A:HEM201 4.1 23.6 0.5
C3B A:HEM201 4.2 23.6 0.5
C2D A:HEM201 4.2 20.5 0.5
C2B A:HEM201 4.2 21.8 0.5
C3D A:HEM201 4.2 21.2 0.5
CB A:MET52 4.2 18.4 1.0
C2A A:HEM201 4.2 21.5 0.5
C3A A:HEM201 4.3 20.7 0.5
C2C A:HEM201 4.3 20.1 0.5
C3C A:HEM201 4.3 22.8 0.5
CB B:MET52 4.3 17.9 1.0
C3B A:HEM201 4.3 19.8 0.5
C2B A:HEM201 4.4 22.6 0.5
C2D A:HEM201 4.4 21.4 0.5
C2A A:HEM201 4.4 23.5 0.5
C3D A:HEM201 4.4 23.6 0.5
C3A A:HEM201 4.4 20.6 0.5

Iron binding site 3 out of 4 in 4tog

Go back to Iron Binding Sites List in 4tog
Iron binding site 3 out of 4 in the 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe201

b:23.5
occ:0.50
 FE C:HEM201 0.0 23.5 0.5
NA C:HEM201 2.0 22.9 0.5
ND C:HEM201 2.1 23.0 0.5
NC C:HEM201 2.1 21.7 0.5
NB C:HEM201 2.1 21.1 0.5
SD C:MET52 2.2 21.7 1.0
C1A C:HEM201 3.0 25.5 0.5
C4D C:HEM201 3.1 25.4 0.5
C4A C:HEM201 3.1 24.8 0.5
C1D C:HEM201 3.1 23.2 0.5
C4C C:HEM201 3.1 24.4 0.5
C1C C:HEM201 3.1 22.5 0.5
C4B C:HEM201 3.1 22.6 0.5
C1B C:HEM201 3.1 23.9 0.5
CE C:MET52 3.3 22.1 1.0
CG C:MET52 3.4 24.1 1.0
CHA C:HEM201 3.4 24.6 0.5
CHD C:HEM201 3.4 24.7 0.5
CHB C:HEM201 3.5 23.9 0.5
CHC C:HEM201 3.5 21.9 0.5
CB C:MET52 4.1 23.5 1.0
C2A C:HEM201 4.2 22.8 0.5
C3A C:HEM201 4.3 24.6 0.5
C3D C:HEM201 4.3 22.8 0.5
C2D C:HEM201 4.3 24.7 0.5
C3C C:HEM201 4.3 20.5 0.5
C2C C:HEM201 4.3 23.5 0.5
C3B C:HEM201 4.3 25.3 0.5
C2B C:HEM201 4.3 20.2 0.5
CD1 C:ILE49 5.0 24.9 1.0

Iron binding site 4 out of 4 in 4tog

Go back to Iron Binding Sites List in 4tog
Iron binding site 4 out of 4 in the 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of 1.80A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 2 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe201

b:24.9
occ:0.50
 FE D:HEM201 0.0 24.9 0.5
NB D:HEM201 2.0 23.2 0.5
NA D:HEM201 2.0 24.3 0.5
NC D:HEM201 2.1 22.8 0.5
ND D:HEM201 2.2 23.8 0.5
SD D:MET52 2.3 22.6 1.0
C1B D:HEM201 3.0 24.3 0.5
C4B D:HEM201 3.0 24.4 0.5
C4A D:HEM201 3.0 23.8 0.5
C1C D:HEM201 3.1 22.9 0.5
C1A D:HEM201 3.1 23.9 0.5
C4C D:HEM201 3.1 24.1 0.5
CE D:MET52 3.1 25.8 1.0
C4D D:HEM201 3.2 24.2 0.5
C1D D:HEM201 3.2 23.9 0.5
CHC D:HEM201 3.4 22.8 0.5
CHB D:HEM201 3.4 21.3 0.5
CHA D:HEM201 3.5 25.8 0.5
CHD D:HEM201 3.5 22.6 0.5
CG D:MET52 3.6 22.9 1.0
C2B D:HEM201 4.2 21.5 0.5
C3B D:HEM201 4.3 22.1 0.5
C3A D:HEM201 4.3 24.9 0.5
C2A D:HEM201 4.3 23.0 0.5
C2C D:HEM201 4.3 23.5 0.5
C3C D:HEM201 4.3 21.6 0.5
C3D D:HEM201 4.4 22.9 0.5
C2D D:HEM201 4.4 25.0 0.5
CB D:MET52 4.4 19.4 1.0

Reference:

H.Yao, H.Rui, R.Kumar, K.Eshelman, S.Lovell, K.P.Battaile, W.Im, M.Rivera. Concerted Motions Networking Pores and Distant Ferroxidase Centers Enable Bacterioferritin Function and Iron Traffic. Biochemistry 2015.
ISSN: ISSN 0006-2960
PubMed: 25640193
DOI: 10.1021/BI501255R
Page generated: Mon Aug 5 11:49:20 2024

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