Iron in PDB 5sx1: Crystal Structure of D141E Variant of B. Pseudomallei Katg

Enzymatic activity of Crystal Structure of D141E Variant of B. Pseudomallei Katg

All present enzymatic activity of Crystal Structure of D141E Variant of B. Pseudomallei Katg:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of D141E Variant of B. Pseudomallei Katg, PDB code: 5sx1 was solved by P.C.Loewen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.739, 116.198, 175.018, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 19.1

Other elements in 5sx1:

The structure of Crystal Structure of D141E Variant of B. Pseudomallei Katg also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of D141E Variant of B. Pseudomallei Katg (pdb code 5sx1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of D141E Variant of B. Pseudomallei Katg, PDB code: 5sx1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5sx1

Go back to Iron Binding Sites List in 5sx1
Iron binding site 1 out of 2 in the Crystal Structure of D141E Variant of B. Pseudomallei Katg


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 D141E Variant of B. Pseudomallei Katg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:15.0
occ:1.00
FE A:HEM801 0.0 15.0 1.0
ND A:HEM801 2.0 16.5 1.0
NC A:HEM801 2.0 14.5 1.0
NA A:HEM801 2.0 16.8 1.0
NB A:HEM801 2.1 18.1 1.0
NE2 A:HIS279 2.1 16.5 1.0
O1 A:OXY804 2.9 33.9 1.0
C1D A:HEM801 3.0 13.8 1.0
C1C A:HEM801 3.0 13.4 1.0
C1B A:HEM801 3.0 17.6 1.0
C4C A:HEM801 3.0 13.6 1.0
C4B A:HEM801 3.1 15.8 1.0
CE1 A:HIS279 3.1 15.5 1.0
C4A A:HEM801 3.1 17.2 1.0
C4D A:HEM801 3.1 14.2 1.0
CD2 A:HIS279 3.1 14.0 1.0
C1A A:HEM801 3.1 14.2 1.0
CHD A:HEM801 3.4 13.1 1.0
CHB A:HEM801 3.4 18.8 1.0
CHC A:HEM801 3.4 14.7 1.0
CHA A:HEM801 3.5 14.2 1.0
O2 A:OXY804 3.7 44.5 1.0
ND1 A:HIS279 4.2 15.9 1.0
C2D A:HEM801 4.3 13.7 1.0
CG A:HIS279 4.3 15.2 1.0
C2B A:HEM801 4.3 19.9 1.0
NE1 A:TRP111 4.3 15.7 1.0
C3C A:HEM801 4.3 13.4 1.0
C2C A:HEM801 4.3 13.2 1.0
C3B A:HEM801 4.3 17.8 1.0
C3D A:HEM801 4.3 14.5 1.0
C3A A:HEM801 4.3 15.2 1.0
C2A A:HEM801 4.3 15.6 1.0
CD1 A:TRP111 4.5 15.3 1.0
O2 A:OXY803 4.6 44.8 1.0
O A:HOH940 4.9 46.7 1.0

Iron binding site 2 out of 2 in 5sx1

Go back to Iron Binding Sites List in 5sx1
Iron binding site 2 out of 2 in the Crystal Structure of D141E Variant of B. Pseudomallei Katg


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 D141E Variant of B. Pseudomallei Katg within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe801

b:14.2
occ:1.00
FE B:HEM801 0.0 14.2 1.0
ND B:HEM801 2.0 13.8 1.0
NC B:HEM801 2.0 12.6 1.0
NB B:HEM801 2.0 13.7 1.0
NA B:HEM801 2.0 13.0 1.0
NE2 B:HIS279 2.1 15.0 1.0
O1 B:OXY804 2.5 39.2 1.0
C1C B:HEM801 3.0 12.0 1.0
C4A B:HEM801 3.0 14.0 1.0
C4C B:HEM801 3.0 13.3 1.0
C4D B:HEM801 3.0 13.4 1.0
C4B B:HEM801 3.0 13.8 1.0
C1B B:HEM801 3.0 15.7 1.0
C1D B:HEM801 3.0 13.4 1.0
C1A B:HEM801 3.1 12.3 1.0
CE1 B:HIS279 3.1 13.6 1.0
CD2 B:HIS279 3.1 14.2 1.0
CHC B:HEM801 3.3 13.1 1.0
CHB B:HEM801 3.4 13.9 1.0
O2 B:OXY804 3.4 50.3 1.0
CHA B:HEM801 3.4 13.1 1.0
CHD B:HEM801 3.4 13.2 1.0
ND1 B:HIS279 4.2 14.8 1.0
C3D B:HEM801 4.2 14.3 1.0
C2C B:HEM801 4.2 12.8 1.0
C3C B:HEM801 4.2 11.9 1.0
C2D B:HEM801 4.3 13.0 1.0
C3A B:HEM801 4.3 13.9 1.0
NE1 B:TRP111 4.3 14.9 1.0
C2B B:HEM801 4.3 13.6 1.0
CG B:HIS279 4.3 13.8 1.0
C3B B:HEM801 4.3 15.2 1.0
C2A B:HEM801 4.3 13.4 1.0
CD1 B:TRP111 4.5 15.1 1.0
O B:HOH913 4.6 43.6 1.0
O2 B:OXY803 4.6 41.2 1.0

Reference:

T.Deemagarn, B.Wiseman, X.Carpena, A.Ivancich, I.Fita, P.C.Loewen. Two Alternative Substrate Paths For Compound I Formation and Reduction in Catalase-Peroxidase Katg From Burkholderia Pseudomallei. Proteins V. 66 219 2007.
ISSN: ESSN 1097-0134
PubMed: 17063492
Page generated: Sun Dec 13 16:11:38 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