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Iron in PDB 3v98: S663D Stable-5-Lox

Enzymatic activity of S663D Stable-5-Lox

All present enzymatic activity of S663D Stable-5-Lox:
1.13.11.34;

Protein crystallography data

The structure of S663D Stable-5-Lox, PDB code: 3v98 was solved by N.C.Gilbert, Z.Rui, D.B.Neau, M.Waight, S.G.Bartlett, W.E.Boeglin, A.R.Brash, M.E.Newcomer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.49 / 2.07
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 55.410, 202.503, 76.971, 90.00, 109.82, 90.00
R / Rfree (%) 16.6 / 19.7

Iron Binding Sites:

The binding sites of Iron atom in the S663D Stable-5-Lox (pdb code 3v98). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the S663D Stable-5-Lox, PDB code: 3v98:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 3v98

Go back to Iron Binding Sites List in 3v98
Iron binding site 1 out of 2 in the S663D Stable-5-Lox


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of S663D Stable-5-Lox within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe701

b:12.4
occ:1.00
NE2 A:HIS550 2.1 15.7 1.0
NE2 A:HIS372 2.1 20.4 1.0
NE2 A:HIS367 2.2 14.2 1.0
O A:HOH1227 2.2 23.0 1.0
O A:ILE673 2.4 24.9 1.0
CE1 A:HIS367 3.0 18.1 1.0
HE1 A:HIS367 3.0 21.6 1.0
CD2 A:HIS550 3.0 11.7 1.0
CD2 A:HIS372 3.1 13.3 1.0
CE1 A:HIS372 3.1 13.6 1.0
CE1 A:HIS550 3.1 15.0 1.0
HD2 A:HIS550 3.2 13.9 1.0
HD2 A:HIS372 3.3 15.9 1.0
HE1 A:HIS372 3.3 16.2 1.0
CD2 A:HIS367 3.3 13.7 1.0
HE1 A:HIS550 3.3 17.9 1.0
C A:ILE673 3.4 29.1 1.0
OD1 A:ASN554 3.4 20.2 1.0
HG13 A:VAL671 3.6 17.9 1.0
OXT A:ILE673 3.6 22.3 1.0
HD2 A:HIS367 3.6 16.3 1.0
HB2 A:ASN554 3.6 18.0 1.0
CG A:ASN554 3.8 16.8 1.0
HG23 A:ILE673 4.1 24.1 1.0
ND1 A:HIS367 4.2 17.3 1.0
CG A:HIS550 4.2 12.4 1.0
ND1 A:HIS550 4.2 14.2 1.0
ND1 A:HIS372 4.2 13.5 1.0
CB A:ASN554 4.2 15.1 1.0
CG A:HIS372 4.3 14.7 1.0
H A:ILE673 4.4 27.1 1.0
CG A:HIS367 4.4 14.3 1.0
CG1 A:VAL671 4.4 15.0 1.0
ND2 A:ASN554 4.5 19.5 1.0
HG11 A:VAL671 4.6 17.9 1.0
HG12 A:VAL671 4.6 17.9 1.0
HD21 A:ASN554 4.7 23.3 1.0
HB3 A:ASN554 4.7 18.0 1.0
CA A:ILE673 4.7 24.0 1.0
HD1 A:HIS367 4.9 20.7 1.0
CG2 A:ILE673 4.9 20.1 1.0
HG22 A:ILE673 4.9 24.1 1.0
N A:ILE673 5.0 22.7 1.0

Iron binding site 2 out of 2 in 3v98

Go back to Iron Binding Sites List in 3v98
Iron binding site 2 out of 2 in the S663D Stable-5-Lox


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of S663D Stable-5-Lox within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe701

b:11.4
occ:1.00
NE2 B:HIS550 2.1 13.2 1.0
NE2 B:HIS372 2.1 15.1 1.0
NE2 B:HIS367 2.2 13.5 1.0
O B:HOH1012 2.3 25.2 1.0
O B:ILE673 2.4 20.9 1.0
CD2 B:HIS550 2.9 13.2 1.0
HD2 B:HIS550 2.9 15.8 1.0
CE1 B:HIS367 3.0 18.5 1.0
HE1 B:HIS367 3.1 22.1 1.0
CD2 B:HIS372 3.1 13.8 1.0
CE1 B:HIS372 3.1 14.0 1.0
HD2 B:HIS372 3.3 16.5 1.0
CE1 B:HIS550 3.3 11.4 1.0
CD2 B:HIS367 3.3 16.9 1.0
HE1 B:HIS372 3.3 16.7 1.0
OD1 B:ASN554 3.3 18.8 1.0
C B:ILE673 3.4 27.3 1.0
HG13 B:VAL671 3.5 17.9 1.0
HD2 B:HIS367 3.6 20.2 1.0
HE1 B:HIS550 3.6 13.6 1.0
OXT B:ILE673 3.6 29.0 1.0
HB2 B:ASN554 3.6 16.9 1.0
CG B:ASN554 3.8 14.8 1.0
CG B:HIS550 4.1 13.7 1.0
ND1 B:HIS367 4.2 19.2 1.0
ND1 B:HIS372 4.2 13.6 1.0
CB B:ASN554 4.2 14.1 1.0
CG B:HIS372 4.2 13.1 1.0
HG23 B:ILE673 4.3 25.4 1.0
ND1 B:HIS550 4.3 12.6 1.0
CG B:HIS367 4.3 16.2 1.0
CG1 B:VAL671 4.4 15.0 1.0
H B:ILE673 4.4 23.4 1.0
ND2 B:ASN554 4.5 13.4 1.0
HG11 B:VAL671 4.5 17.9 1.0
HG12 B:VAL671 4.6 17.9 1.0
HD21 B:ASN554 4.7 16.0 1.0
HB3 B:ASN554 4.7 16.9 1.0
CA B:ILE673 4.8 22.1 1.0
HD1 B:HIS367 4.9 22.9 1.0
HD1 B:HIS372 5.0 16.2 1.0
N B:ILE673 5.0 19.6 1.0
HD22 B:LEU607 5.0 40.3 1.0

Reference:

N.C.Gilbert, Z.Rui, D.B.Neau, M.T.Waight, S.G.Bartlett, W.E.Boeglin, A.R.Brash, M.E.Newcomer. Conversion of Human 5-Lipoxygenase to A 15-Lipoxygenase By A Point Mutation to Mimic Phosphorylation at Serine-663. Faseb J. V. 26 3222 2012.
ISSN: ISSN 0892-6638
PubMed: 22516296
DOI: 10.1096/FJ.12-205286
Page generated: Sun Dec 13 15:24:14 2020

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