Atomistry » Iron » PDB 4tof-4ud2 » 4tof
Atomistry »
  Iron »
    PDB 4tof-4ud2 »
      4tof »

Iron in PDB 4tof: 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 From Pseudomonas Aeruginosa

Enzymatic activity of 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 From Pseudomonas Aeruginosa

All present enzymatic activity of 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 From Pseudomonas Aeruginosa:
1.16.3.1;

Protein crystallography data

The structure of 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 From Pseudomonas Aeruginosa, PDB code: 4tof 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) 38.10 / 1.65
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 158.568, 158.568, 152.381, 90.00, 90.00, 120.00
R / Rfree (%) 14.5 / 16.2

Other elements in 4tof:

The structure of 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 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 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 From Pseudomonas Aeruginosa (pdb code 4tof). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 From Pseudomonas Aeruginosa, PDB code: 4tof:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4tof

Go back to Iron Binding Sites List in 4tof
Iron binding site 1 out of 4 in the 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 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 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:16.5
occ:0.50
 FE A:HEM201 0.0 16.5 0.5
FE A:HEM201 0.3 16.6 0.5
ND A:HEM201 1.8 15.5 0.5
NC A:HEM201 1.9 16.1 0.5
NA A:HEM201 2.0 15.9 0.5
NB A:HEM201 2.0 15.7 0.5
NC A:HEM201 2.1 15.4 0.5
ND A:HEM201 2.1 17.3 0.5
NA A:HEM201 2.2 17.4 0.5
NB A:HEM201 2.3 15.2 0.5
SD A:MET52 2.4 16.3 1.0
SD B:MET52 2.4 15.4 1.0
C1D A:HEM201 2.8 16.4 0.5
C4C A:HEM201 2.8 15.4 0.5
C4D A:HEM201 2.9 17.2 0.5
C1C A:HEM201 3.0 17.9 0.5
C4A A:HEM201 3.0 16.7 0.5
C1A A:HEM201 3.0 17.2 0.5
C1B A:HEM201 3.1 16.0 0.5
C4B A:HEM201 3.1 18.4 0.5
C4D A:HEM201 3.1 17.4 0.5
C1C A:HEM201 3.1 15.5 0.5
C1D A:HEM201 3.1 17.7 0.5
C4C A:HEM201 3.1 15.6 0.5
C1A A:HEM201 3.1 17.4 0.5
CHD A:HEM201 3.1 17.6 0.5
CE A:MET52 3.3 17.9 1.0
C4B A:HEM201 3.3 16.1 0.5
C4A A:HEM201 3.3 17.9 0.5
C1B A:HEM201 3.4 15.4 0.5
CHA A:HEM201 3.4 19.0 0.5
CHB A:HEM201 3.4 17.2 0.5
CHA A:HEM201 3.4 19.0 0.5
CE B:MET52 3.4 17.6 1.0
CHC A:HEM201 3.4 19.1 0.5
CHD A:HEM201 3.5 18.2 0.5
CG B:MET52 3.5 14.5 1.0
CHC A:HEM201 3.5 19.1 0.5
CG A:MET52 3.6 14.8 1.0
CHB A:HEM201 3.7 17.9 0.5
C2D A:HEM201 4.0 17.9 0.5
C3C A:HEM201 4.1 14.9 0.5
C3D A:HEM201 4.1 17.8 0.5
C2C A:HEM201 4.2 16.4 0.5
CB B:MET52 4.2 13.5 1.0
C3A A:HEM201 4.2 18.1 0.5
C2A A:HEM201 4.2 17.8 0.5
C3B A:HEM201 4.3 16.0 0.5
C2B A:HEM201 4.3 15.5 0.5
C3D A:HEM201 4.3 19.0 0.5
C2C A:HEM201 4.3 17.7 0.5
C3C A:HEM201 4.3 17.2 0.5
C2D A:HEM201 4.3 19.0 0.5
CB A:MET52 4.3 13.1 1.0
C2A A:HEM201 4.4 19.0 0.5
C3A A:HEM201 4.5 19.0 0.5
C3B A:HEM201 4.5 18.5 0.5
C2B A:HEM201 4.6 16.6 0.5

Iron binding site 2 out of 4 in 4tof

Go back to Iron Binding Sites List in 4tof
Iron binding site 2 out of 4 in the 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 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 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:16.6
occ:0.50
 FE A:HEM201 0.0 16.6 0.5
FE A:HEM201 0.3 16.5 0.5
NC A:HEM201 1.8 15.4 0.5
ND A:HEM201 1.9 17.3 0.5
NC A:HEM201 2.0 16.1 0.5
NA A:HEM201 2.0 17.4 0.5
NB A:HEM201 2.0 15.2 0.5
ND A:HEM201 2.1 15.5 0.5
NB A:HEM201 2.2 15.7 0.5
NA A:HEM201 2.3 15.9 0.5
SD B:MET52 2.4 15.4 1.0
SD A:MET52 2.4 16.3 1.0
C4C A:HEM201 2.8 15.6 0.5
C1D A:HEM201 2.8 17.7 0.5
C1C A:HEM201 2.9 15.5 0.5
C1C A:HEM201 3.0 17.9 0.5
C4D A:HEM201 3.0 17.4 0.5
C4C A:HEM201 3.0 15.4 0.5
C4B A:HEM201 3.0 16.1 0.5
C4A A:HEM201 3.0 17.9 0.5
C1B A:HEM201 3.1 15.4 0.5
C1A A:HEM201 3.1 17.4 0.5
C1D A:HEM201 3.1 16.4 0.5
C4D A:HEM201 3.1 17.2 0.5
C4B A:HEM201 3.1 18.4 0.5
CHD A:HEM201 3.1 18.2 0.5
CE B:MET52 3.2 17.6 1.0
C1A A:HEM201 3.2 17.2 0.5
C1B A:HEM201 3.3 16.0 0.5
C4A A:HEM201 3.3 16.7 0.5
CHC A:HEM201 3.4 19.1 0.5
CHC A:HEM201 3.4 19.1 0.5
CHD A:HEM201 3.4 17.6 0.5
CE A:MET52 3.4 17.9 1.0
CHB A:HEM201 3.4 17.9 0.5
CHA A:HEM201 3.5 19.0 0.5
CHA A:HEM201 3.5 19.0 0.5
CG A:MET52 3.5 14.8 1.0
CG B:MET52 3.5 14.5 1.0
CHB A:HEM201 3.7 17.2 0.5
C3C A:HEM201 4.0 17.2 0.5
C2C A:HEM201 4.1 17.7 0.5
C2D A:HEM201 4.1 19.0 0.5
C3D A:HEM201 4.2 19.0 0.5
CB A:MET52 4.2 13.1 1.0
C2C A:HEM201 4.2 16.4 0.5
C2A A:HEM201 4.3 19.0 0.5
C3A A:HEM201 4.3 19.0 0.5
C3C A:HEM201 4.3 14.9 0.5
C2B A:HEM201 4.3 16.6 0.5
C3B A:HEM201 4.3 18.5 0.5
CB B:MET52 4.3 13.5 1.0
C2D A:HEM201 4.3 17.9 0.5
C3D A:HEM201 4.3 17.8 0.5
C3B A:HEM201 4.4 16.0 0.5
C2B A:HEM201 4.5 15.5 0.5
C2A A:HEM201 4.5 17.8 0.5
C3A A:HEM201 4.5 18.1 0.5

Iron binding site 3 out of 4 in 4tof

Go back to Iron Binding Sites List in 4tof
Iron binding site 3 out of 4 in the 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 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 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe201

b:17.3
occ:0.50
 FE C:HEM201 0.0 17.3 0.5
NB C:HEM201 2.0 17.4 0.5
NA C:HEM201 2.0 16.2 0.5
NC C:HEM201 2.1 16.2 0.5
ND C:HEM201 2.1 16.4 0.5
SD C:MET52 2.2 16.5 1.0
C1A C:HEM201 3.1 16.6 0.5
C4B C:HEM201 3.1 19.9 0.5
C1B C:HEM201 3.1 17.5 0.5
C4A C:HEM201 3.1 18.9 0.5
C1C C:HEM201 3.1 18.4 0.5
C1D C:HEM201 3.1 19.2 0.5
C4D C:HEM201 3.1 16.6 0.5
C4C C:HEM201 3.1 17.8 0.5
CE C:MET52 3.2 18.7 1.0
CG C:MET52 3.3 14.7 1.0
CHA C:HEM201 3.4 18.0 0.5
CHC C:HEM201 3.4 19.2 0.5
CHD C:HEM201 3.4 19.6 0.5
CHB C:HEM201 3.4 18.9 0.5
CB C:MET52 4.0 14.8 1.0
C3A C:HEM201 4.3 17.4 0.5
C2A C:HEM201 4.3 17.8 0.5
C2B C:HEM201 4.3 16.1 0.5
C3B C:HEM201 4.3 20.0 0.5
C2C C:HEM201 4.3 18.9 0.5
C2D C:HEM201 4.3 17.4 0.5
C3C C:HEM201 4.3 16.3 0.5
C3D C:HEM201 4.3 17.8 0.5

Iron binding site 4 out of 4 in 4tof

Go back to Iron Binding Sites List in 4tof
Iron binding site 4 out of 4 in the 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 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 1.65A Resolution Structure of Bfrb (C89S, K96C) Crystal Form 1 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe201

b:16.9
occ:0.50
 FE D:HEM201 0.0 16.9 0.5
NC D:HEM201 2.0 17.7 0.5
ND D:HEM201 2.0 17.7 0.5
NB D:HEM201 2.1 17.5 0.5
NA D:HEM201 2.1 18.2 0.5
SD D:MET52 2.4 16.8 1.0
C4C D:HEM201 3.0 17.8 0.5
C1D D:HEM201 3.0 19.4 0.5
C1C D:HEM201 3.0 17.9 0.5
C4D D:HEM201 3.0 17.8 0.5
C1A D:HEM201 3.1 17.0 0.5
C4B D:HEM201 3.1 18.0 0.5
C1B D:HEM201 3.2 17.8 0.5
C4A D:HEM201 3.2 18.5 0.5
CHD D:HEM201 3.3 17.3 0.5
CHA D:HEM201 3.4 18.5 0.5
CHC D:HEM201 3.4 18.3 0.5
CE D:MET52 3.5 17.7 1.0
CG D:MET52 3.5 16.4 1.0
CHB D:HEM201 3.6 17.1 0.5
CB D:MET52 4.1 15.1 1.0
C3C D:HEM201 4.2 17.3 0.5
C2D D:HEM201 4.2 18.5 0.5
C2C D:HEM201 4.2 18.9 0.5
C3D D:HEM201 4.3 18.9 0.5
C2A D:HEM201 4.3 19.6 0.5
C3B D:HEM201 4.4 18.2 0.5
C3A D:HEM201 4.4 17.1 0.5
C2B D:HEM201 4.4 17.5 0.5

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy