Iron in PDB 7opn: Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene

Enzymatic activity of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene

All present enzymatic activity of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene:
1.2.3.1;

Protein crystallography data

The structure of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene, PDB code: 7opn was solved by C.Mota, C.Coelho, T.Santos Silva, M.J.Romao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.01 / 2.60
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 149.528, 149.528, 269.488, 90, 90, 90
R / Rfree (%) 20.6 / 24.1

Other elements in 7opn:

The structure of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene also contains other interesting chemical elements:

Molybdenum (Mo) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene (pdb code 7opn). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene, PDB code: 7opn:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 7opn

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Iron binding site 1 out of 8 in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe3001

b:44.0
occ:1.00
 FE1 A:FES3001 0.0 44.0 1.0
S2 A:FES3001 2.2 43.3 1.0
S1 A:FES3001 2.2 36.6 1.0
SG A:CYS117 2.3 42.1 1.0
SG A:CYS149 2.3 44.5 1.0
FE2 A:FES3001 2.7 36.9 1.0
CB A:CYS117 3.4 39.4 1.0
CB A:CYS149 3.4 43.2 1.0
CA A:CYS149 3.8 41.4 1.0
N A:ARG150 4.2 43.6 1.0
N A:CYS117 4.2 41.3 1.0
CB A:CYS151 4.3 43.1 1.0
CA A:CYS117 4.4 39.6 1.0
N A:CYS151 4.4 43.7 1.0
C A:CYS149 4.4 42.3 1.0
SG A:CYS151 4.5 45.4 1.0
SG A:CYS114 4.6 45.0 1.0
CG2 A:THR152 4.6 42.9 1.0
O A:LEU148 4.9 46.2 1.0
CA A:CYS151 4.9 43.4 1.0
C A:CYS117 5.0 39.2 1.0

Iron binding site 2 out of 8 in 7opn

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Iron binding site 2 out of 8 in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe3001

b:36.9
occ:1.00
 FE2 A:FES3001 0.0 36.9 1.0
S2 A:FES3001 2.2 43.3 1.0
S1 A:FES3001 2.2 36.6 1.0
SG A:CYS114 2.3 45.0 1.0
SG A:CYS151 2.3 45.4 1.0
FE1 A:FES3001 2.7 44.0 1.0
CB A:CYS151 3.2 43.1 1.0
CB A:CYS114 3.4 38.5 1.0
N A:CYS114 3.7 41.3 1.0
CA A:CYS114 4.0 39.1 1.0
N A:GLY115 4.0 37.0 1.0
N A:CYS151 4.1 43.7 1.0
SG A:CYS149 4.3 44.5 1.0
CA A:CYS151 4.3 43.4 1.0
C A:CYS114 4.3 36.5 1.0
N A:PHE116 4.5 35.8 1.0
SG A:CYS117 4.7 42.1 1.0
N A:ARG150 4.7 43.6 1.0
CB A:GLN113 4.8 40.1 1.0
C A:GLN113 4.8 40.6 1.0
N A:GLN113 5.0 41.3 1.0
N A:CYS117 5.0 41.3 1.0
C A:ARG150 5.0 41.6 1.0

Iron binding site 3 out of 8 in 7opn

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Iron binding site 3 out of 8 in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe3002

b:58.0
occ:0.70
 FE1 A:FES3002 0.0 58.0 0.7
S1 A:FES3002 2.2 58.1 0.7
S2 A:FES3002 2.2 58.2 0.7
SG A:CYS49 2.3 57.5 1.0
FE2 A:FES3002 2.7 67.8 0.7
SG A:CYS44 3.0 67.4 1.0
N A:CYS44 3.4 54.6 1.0
CB A:CYS49 3.6 46.3 1.0
N A:CYS49 3.7 52.4 1.0
N A:GLY50 3.8 47.3 1.0
N A:GLY45 3.9 57.6 1.0
CA A:CYS49 4.0 47.1 1.0
CB A:CYS44 4.0 58.0 1.0
CA A:GLY43 4.0 53.2 1.0
C A:GLY43 4.1 57.4 1.0
N A:GLY43 4.1 50.3 1.0
CA A:CYS44 4.1 57.0 1.0
N A:ALA51 4.1 43.7 1.0
C A:CYS49 4.3 45.4 1.0
SG A:CYS52 4.4 50.9 1.0
N A:GLY48 4.4 53.9 1.0
C A:CYS44 4.4 59.6 1.0
N A:GLY47 4.6 54.9 1.0
CB A:ALA51 4.7 40.0 1.0
CA A:GLY50 4.8 43.1 1.0
SG A:CYS74 4.8 56.5 1.0
CA A:GLY45 4.9 58.6 1.0
N A:CYS52 4.9 45.2 1.0
N A:GLY46 4.9 63.1 1.0
C A:GLY48 4.9 52.7 1.0
C A:GLY50 4.9 43.9 1.0
CA A:ALA51 4.9 41.7 1.0
CA A:GLY47 5.0 52.1 1.0
C A:GLY47 5.0 55.1 1.0

Iron binding site 4 out of 8 in 7opn

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Iron binding site 4 out of 8 in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe3002

b:67.8
occ:0.70
 FE2 A:FES3002 0.0 67.8 0.7
S2 A:FES3002 2.2 58.2 0.7
S1 A:FES3002 2.2 58.1 0.7
SG A:CYS52 2.3 50.9 1.0
SG A:CYS74 2.3 56.5 1.0
FE1 A:FES3002 2.7 58.0 0.7
CB A:CYS74 3.4 52.3 1.0
CB A:CYS52 3.7 42.4 1.0
N A:GLY47 4.1 54.9 1.0
N A:GLY45 4.2 57.6 1.0
CA A:GLY47 4.3 52.1 1.0
CA A:GLY45 4.4 58.6 1.0
CB A:ASN72 4.4 48.5 1.0
N A:CYS52 4.5 45.2 1.0
N A:CYS74 4.5 45.1 1.0
CG A:ASN72 4.6 49.8 1.0
CA A:CYS74 4.6 48.0 1.0
OD1 A:ASN72 4.6 50.2 1.0
N A:GLY46 4.7 63.1 1.0
CA A:CYS52 4.7 43.0 1.0
C A:GLY45 4.8 61.9 1.0
SG A:CYS49 4.8 57.5 1.0
SG A:CYS44 4.9 67.4 1.0

Iron binding site 5 out of 8 in 7opn

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Iron binding site 5 out of 8 in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe3001

b:46.0
occ:1.00
 FE1 B:FES3001 0.0 46.0 1.0
S2 B:FES3001 2.2 40.3 1.0
S1 B:FES3001 2.2 47.1 1.0
SG B:CYS117 2.3 46.1 1.0
SG B:CYS149 2.3 44.2 1.0
FE2 B:FES3001 2.7 40.9 1.0
CB B:CYS149 3.4 44.2 1.0
CB B:CYS117 3.5 40.4 1.0
CA B:CYS149 3.9 44.5 1.0
N B:ARG150 4.2 41.9 1.0
N B:CYS117 4.2 39.5 1.0
CB B:CYS151 4.3 45.0 1.0
N B:CYS151 4.4 44.1 1.0
CA B:CYS117 4.4 39.0 1.0
SG B:CYS151 4.4 46.2 1.0
C B:CYS149 4.5 42.6 1.0
SG B:CYS114 4.6 45.2 1.0
CG2 B:THR152 4.6 44.5 1.0
N B:GLY115 4.9 41.2 1.0
O B:LEU148 4.9 43.7 1.0
CA B:CYS151 5.0 44.4 1.0
N B:PHE116 5.0 38.9 1.0

Iron binding site 6 out of 8 in 7opn

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Iron binding site 6 out of 8 in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe3001

b:40.9
occ:1.00
 FE2 B:FES3001 0.0 40.9 1.0
S2 B:FES3001 2.2 40.3 1.0
S1 B:FES3001 2.2 47.1 1.0
SG B:CYS114 2.3 45.2 1.0
SG B:CYS151 2.3 46.2 1.0
FE1 B:FES3001 2.7 46.0 1.0
CB B:CYS151 3.2 45.0 1.0
CB B:CYS114 3.4 39.5 1.0
O B:HOH3151 3.6 40.1 1.0
N B:CYS114 3.7 43.5 1.0
N B:GLY115 4.0 41.2 1.0
CA B:CYS114 4.0 40.6 1.0
N B:CYS151 4.1 44.1 1.0
SG B:CYS149 4.2 44.2 1.0
CA B:CYS151 4.3 44.4 1.0
C B:CYS114 4.3 40.7 1.0
N B:PHE116 4.5 38.9 1.0
N B:ARG150 4.7 41.9 1.0
SG B:CYS117 4.7 46.1 1.0
C B:GLN113 4.9 44.5 1.0
CB B:GLN113 4.9 45.6 1.0
C B:ARG150 4.9 42.4 1.0
CA B:GLY115 5.0 40.4 1.0

Iron binding site 7 out of 8 in 7opn

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Iron binding site 7 out of 8 in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe3002

b:56.9
occ:0.68
 FE1 B:FES3002 0.0 56.9 0.7
S1 B:FES3002 2.2 58.2 0.7
S2 B:FES3002 2.2 59.7 0.7
SG B:CYS49 2.3 58.4 1.0
FE2 B:FES3002 2.7 66.4 0.7
SG B:CYS44 3.0 69.4 1.0
N B:CYS44 3.4 54.3 1.0
CB B:CYS49 3.7 49.7 1.0
N B:CYS49 3.8 55.9 1.0
N B:GLY50 3.8 50.5 1.0
N B:GLY45 3.9 57.9 1.0
CA B:GLY43 4.0 52.2 1.0
CA B:CYS49 4.1 53.3 1.0
CB B:CYS44 4.1 56.2 1.0
C B:GLY43 4.1 55.7 1.0
N B:GLY43 4.1 50.7 1.0
N B:ALA51 4.1 49.9 1.0
CA B:CYS44 4.2 58.8 1.0
C B:CYS49 4.3 50.8 1.0
SG B:CYS52 4.3 52.1 1.0
N B:GLY48 4.4 56.2 1.0
C B:CYS44 4.5 60.4 1.0
N B:GLY47 4.6 57.9 1.0
CA B:GLY50 4.7 48.9 1.0
CB B:ALA51 4.7 41.2 1.0
SG B:CYS74 4.8 53.8 1.0
N B:CYS52 4.8 48.0 1.0
CA B:GLY45 4.8 59.5 1.0
CA B:GLY47 4.8 55.1 1.0
C B:GLY50 4.9 49.4 1.0
C B:GLY48 4.9 57.2 1.0
C B:GLY47 4.9 58.8 1.0
N B:GLY46 4.9 66.0 1.0
CA B:ALA51 4.9 46.8 1.0

Iron binding site 8 out of 8 in 7opn

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Iron binding site 8 out of 8 in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe3002

b:66.4
occ:0.68
 FE2 B:FES3002 0.0 66.4 0.7
S2 B:FES3002 2.2 59.7 0.7
S1 B:FES3002 2.2 58.2 0.7
SG B:CYS52 2.3 52.1 1.0
SG B:CYS74 2.3 53.8 1.0
FE1 B:FES3002 2.7 56.9 0.7
CB B:CYS74 3.4 54.3 1.0
CB B:CYS52 3.8 45.9 1.0
N B:GLY47 4.1 57.9 1.0
N B:GLY45 4.2 57.9 1.0
CA B:GLY47 4.3 55.1 1.0
CA B:GLY45 4.4 59.5 1.0
CB B:ASN72 4.4 48.5 1.0
N B:CYS74 4.4 45.8 1.0
N B:CYS52 4.5 48.0 1.0
CA B:CYS74 4.5 48.3 1.0
OD1 B:ASN72 4.6 49.7 1.0
CG B:ASN72 4.6 51.0 1.0
N B:GLY46 4.7 66.0 1.0
C B:GLY45 4.7 65.7 1.0
CA B:CYS52 4.7 44.5 1.0
SG B:CYS49 4.9 58.4 1.0
SG B:CYS44 4.9 69.4 1.0

Reference:

C.Mota, A.Diniz, C.Coelho, T.Santos-Silva, M.Esmaeeli, S.Leimkuhler, E.J.Cabrita, F.Marcelo, M.J.Romao. Interrogating the Inhibition Mechanisms of Human Aldehyde Oxidase By X-Ray Crystallography and uc(Nmr) Spectroscopy: the Raloxifene Case. J.Med.Chem. 2021.
ISSN: ISSN 0022-2623
PubMed: 34415167
DOI: 10.1021/ACS.JMEDCHEM.1C01125
Page generated: Fri Sep 24 14:18:56 2021

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