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Iron in PDB 3o8y: Stable-5-Lipoxygenase

Enzymatic activity of Stable-5-Lipoxygenase

All present enzymatic activity of Stable-5-Lipoxygenase:
1.13.11.34;

Protein crystallography data

The structure of Stable-5-Lipoxygenase, PDB code: 3o8y was solved by M.E.Newcomer, N.C.Gilbert, S.G.Bartlett, M.T.Waight, D.B.Neau, W.E.Boeglin, A.R.Brash, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.77 / 2.39
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 55.170, 202.890, 76.800, 90.00, 109.56, 90.00
R / Rfree (%) 18.2 / 21

Iron Binding Sites:

The binding sites of Iron atom in the Stable-5-Lipoxygenase (pdb code 3o8y). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Stable-5-Lipoxygenase, PDB code: 3o8y:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 3o8y

Go back to Iron Binding Sites List in 3o8y
Iron binding site 1 out of 2 in the Stable-5-Lipoxygenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Stable-5-Lipoxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1

b:17.9
occ:1.00
NE2 A:HIS372 2.1 19.4 1.0
NE2 A:HIS550 2.2 20.8 1.0
O A:ILE673 2.2 43.5 1.0
NE2 A:HIS367 2.2 22.5 1.0
CE1 A:HIS372 3.0 18.3 1.0
CE1 A:HIS367 3.0 24.6 1.0
HE1 A:HIS367 3.1 29.4 1.0
CD2 A:HIS550 3.1 16.2 1.0
HE1 A:HIS372 3.1 21.9 1.0
CD2 A:HIS372 3.2 19.1 1.0
C A:ILE673 3.2 46.1 1.0
OD1 A:ASN554 3.2 22.5 1.0
HD2 A:HIS550 3.2 19.4 1.0
CE1 A:HIS550 3.2 17.8 1.0
CD2 A:HIS367 3.3 19.5 1.0
OXT A:ILE673 3.3 43.3 1.0
HD2 A:HIS372 3.4 22.8 1.0
HE1 A:HIS550 3.5 21.3 1.0
O A:HOH906 3.6 35.7 1.0
HD2 A:HIS367 3.6 23.3 1.0
HB2 A:ASN554 3.7 18.9 1.0
HG13 A:VAL671 3.7 21.7 1.0
CG A:ASN554 3.8 21.0 1.0
ND1 A:HIS372 4.2 14.0 1.0
ND1 A:HIS367 4.2 27.2 1.0
H A:ILE673 4.2 40.7 1.0
HG23 A:ILE673 4.2 30.6 1.0
CG A:HIS372 4.3 18.1 1.0
CB A:ASN554 4.3 15.8 1.0
CG A:HIS550 4.3 16.1 1.0
ND1 A:HIS550 4.3 15.8 1.0
CG A:HIS367 4.4 22.3 1.0
CG1 A:VAL671 4.5 18.1 1.0
CA A:ILE673 4.5 41.9 1.0
ND2 A:ASN554 4.6 18.1 1.0
HG12 A:VAL671 4.6 21.7 1.0
HG11 A:VAL671 4.6 21.7 1.0
HD21 A:ASN554 4.7 21.6 1.0
N A:ILE673 4.8 34.0 1.0
HB3 A:ASN554 4.8 18.9 1.0
HD22 A:LEU607 4.8 36.1 1.0
HD1 A:HIS372 4.9 16.7 1.0
HD1 A:HIS367 4.9 32.6 1.0
CG2 A:ILE673 5.0 25.6 1.0

Iron binding site 2 out of 2 in 3o8y

Go back to Iron Binding Sites List in 3o8y
Iron binding site 2 out of 2 in the Stable-5-Lipoxygenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Stable-5-Lipoxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe674

b:17.6
occ:1.00
NE2 B:HIS550 2.1 19.9 1.0
NE2 B:HIS372 2.2 20.9 1.0
O B:ILE673 2.2 43.4 1.0
NE2 B:HIS367 2.3 22.5 1.0
CE1 B:HIS372 3.1 18.4 1.0
CE1 B:HIS367 3.1 23.3 1.0
CD2 B:HIS550 3.1 16.0 1.0
HE1 B:HIS367 3.1 27.8 1.0
CE1 B:HIS550 3.2 18.7 1.0
C B:ILE673 3.2 46.4 1.0
OD1 B:ASN554 3.2 20.8 1.0
HE1 B:HIS372 3.2 21.9 1.0
CD2 B:HIS372 3.2 18.4 1.0
HD2 B:HIS550 3.2 19.1 1.0
CD2 B:HIS367 3.4 19.5 1.0
OXT B:ILE673 3.4 41.8 1.0
HE1 B:HIS550 3.4 22.4 1.0
HD2 B:HIS372 3.4 22.1 1.0
HB2 B:ASN554 3.6 19.7 1.0
HD2 B:HIS367 3.6 23.3 1.0
HG13 B:VAL671 3.7 22.3 1.0
CG B:ASN554 3.7 20.2 1.0
H B:ILE673 4.2 38.1 1.0
HG23 B:ILE673 4.2 32.5 1.0
CB B:ASN554 4.2 16.5 1.0
ND1 B:HIS372 4.2 14.7 1.0
ND1 B:HIS367 4.2 25.3 1.0
CG B:HIS550 4.2 14.9 1.0
ND1 B:HIS550 4.3 14.9 1.0
CG B:HIS372 4.3 17.9 1.0
CG B:HIS367 4.4 20.8 1.0
CG1 B:VAL671 4.5 18.6 1.0
CA B:ILE673 4.5 40.6 1.0
ND2 B:ASN554 4.5 17.4 1.0
HG12 B:VAL671 4.7 22.3 1.0
HG11 B:VAL671 4.7 22.3 1.0
HD21 B:ASN554 4.7 20.8 1.0
HB3 B:ASN554 4.7 19.7 1.0
N B:ILE673 4.8 31.8 1.0
HD22 B:LEU607 4.9 34.1 1.0
CG2 B:ILE673 5.0 27.2 1.0
HG22 B:ILE673 5.0 32.5 1.0
HD1 B:HIS372 5.0 17.5 1.0
HD1 B:HIS367 5.0 30.3 1.0

Reference:

N.C.Gilbert, S.G.Bartlett, M.T.Waight, D.B.Neau, W.E.Boeglin, A.R.Brash, M.E.Newcomer. The Structure of Human 5-Lipoxygenase. Science V. 331 217 2011.
ISSN: ISSN 0036-8075
PubMed: 21233389
DOI: 10.1126/SCIENCE.1197203
Page generated: Sun Aug 4 17:01:25 2024

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