Atomistry » Iron » PDB 5m3l-5mkq » 5mef
Atomistry »
  Iron »
    PDB 5m3l-5mkq »
      5mef »

Iron in PDB 5mef: Cyanothece Lipoxygenase 2 (CSPLOX2) Variant - L304F

Enzymatic activity of Cyanothece Lipoxygenase 2 (CSPLOX2) Variant - L304F

All present enzymatic activity of Cyanothece Lipoxygenase 2 (CSPLOX2) Variant - L304F:
1.13.11.33;

Protein crystallography data

The structure of Cyanothece Lipoxygenase 2 (CSPLOX2) Variant - L304F, PDB code: 5mef was solved by J.Newie, P.Neumann, M.Werner, R.A.Mata, R.Ficner, I.Feussner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.20 / 2.36
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.400, 166.260, 166.740, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 21.6

Other elements in 5mef:

The structure of Cyanothece Lipoxygenase 2 (CSPLOX2) Variant - L304F also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Cyanothece Lipoxygenase 2 (CSPLOX2) Variant - L304F (pdb code 5mef). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cyanothece Lipoxygenase 2 (CSPLOX2) Variant - L304F, PDB code: 5mef:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5mef

Go back to Iron Binding Sites List in 5mef
Iron binding site 1 out of 2 in the Cyanothece Lipoxygenase 2 (CSPLOX2) Variant - L304F


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cyanothece Lipoxygenase 2 (CSPLOX2) Variant - L304F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1001

b:62.5
occ:0.94
O A:HOH1225 2.1 61.5 0.8
NE2 A:HIS449 2.3 40.1 1.0
NE2 A:HIS262 2.3 49.0 1.0
O A:ILE569 2.4 48.6 1.0
NE2 A:HIS257 2.4 49.1 1.0
OD1 A:ASN453 2.4 44.5 1.0
CE1 A:HIS262 3.0 48.5 1.0
CE1 A:HIS449 3.2 40.5 1.0
CE1 A:HIS257 3.2 48.7 1.0
CD2 A:HIS449 3.3 39.4 1.0
CG A:ASN453 3.3 42.1 1.0
C A:ILE569 3.4 48.3 1.0
CD2 A:HIS257 3.5 48.3 1.0
CD2 A:HIS262 3.5 48.3 1.0
OXT A:ILE569 3.7 48.6 1.0
CB A:ASN453 3.8 41.2 1.0
ND1 A:HIS262 4.2 48.7 1.0
ND1 A:HIS449 4.3 40.4 1.0
ND1 A:HIS257 4.4 48.1 1.0
ND2 A:ASN453 4.4 41.3 1.0
CG A:HIS449 4.4 40.7 1.0
CG A:HIS262 4.5 48.4 1.0
CG A:HIS257 4.6 47.5 1.0
CA A:ILE569 4.7 46.8 1.0
CG2 A:ILE569 4.9 46.2 1.0
N A:ILE569 4.9 46.0 1.0
CA A:ASN453 4.9 42.0 1.0
CD2 A:LEU506 5.0 43.4 1.0

Iron binding site 2 out of 2 in 5mef

Go back to Iron Binding Sites List in 5mef
Iron binding site 2 out of 2 in the Cyanothece Lipoxygenase 2 (CSPLOX2) Variant - L304F


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cyanothece Lipoxygenase 2 (CSPLOX2) Variant - L304F within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1001

b:65.4
occ:0.95
O B:HOH1174 2.1 68.2 0.8
OD1 B:ASN453 2.3 42.7 1.0
NE2 B:HIS257 2.3 45.4 1.0
O B:ILE569 2.3 49.4 1.0
NE2 B:HIS262 2.4 53.1 1.0
NE2 B:HIS449 2.4 41.3 1.0
CE1 B:HIS262 3.1 53.5 1.0
CE1 B:HIS257 3.2 44.3 1.0
CD2 B:HIS449 3.2 39.6 1.0
CG B:ASN453 3.3 39.5 1.0
C B:ILE569 3.4 48.6 1.0
CD2 B:HIS257 3.4 44.8 1.0
CE1 B:HIS449 3.5 41.8 1.0
CD2 B:HIS262 3.6 52.8 1.0
OXT B:ILE569 3.7 48.2 1.0
CB B:ASN453 3.9 39.1 1.0
ND1 B:HIS262 4.3 53.6 1.0
ND1 B:HIS257 4.4 44.7 1.0
ND2 B:ASN453 4.4 37.6 1.0
CG B:HIS449 4.4 41.9 1.0
CG B:HIS257 4.5 44.7 1.0
ND1 B:HIS449 4.5 41.5 1.0
CG B:HIS262 4.6 52.4 1.0
CA B:ILE569 4.7 47.4 1.0
CG2 B:ILE569 4.9 46.3 1.0
N B:ILE569 4.9 46.6 1.0
CA B:ASN453 5.0 40.0 1.0

Reference:

J.Newie, P.Neumann, M.Werner, R.A.Mata, R.Ficner, I.Feussner. Lipoxygenase 2 From Cyanothece Sp. Controls Dioxygen Insertion By Steric Shielding and Substrate Fixation. Sci Rep V. 7 2069 2017.
ISSN: ESSN 2045-2322
PubMed: 28522865
DOI: 10.1038/S41598-017-02153-W
Page generated: Tue Aug 6 05:50:40 2024

Last articles

Cl in 3S8O
Cl in 3S92
Cl in 3S91
Cl in 3S6L
Cl in 3S81
Cl in 3S8N
Cl in 3S8L
Cl in 3S7X
Cl in 3S2Z
Cl in 3S7I
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy