Iron in PDB 6q6q: Human Aldehyde Oxidase Snp G1269R
Enzymatic activity of Human Aldehyde Oxidase Snp G1269R
All present enzymatic activity of Human Aldehyde Oxidase Snp G1269R:
1.2.3.1;
Protein crystallography data
The structure of Human Aldehyde Oxidase Snp G1269R, PDB code: 6q6q
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)
|
46.86 /
3.10
|
Space group
|
P 42 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
148.197,
148.197,
132.204,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.2 /
23.6
|
Iron Binding Sites:
The binding sites of Iron atom in the Human Aldehyde Oxidase Snp G1269R
(pdb code 6q6q). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Human Aldehyde Oxidase Snp G1269R, PDB code: 6q6q:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 6q6q
Go back to
Iron Binding Sites List in 6q6q
Iron binding site 1 out
of 4 in the Human Aldehyde Oxidase Snp G1269R
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 G1269R within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe3001
b:58.8
occ:1.00
|
FE1
|
A:FES3001
|
0.0
|
58.8
|
1.0
|
SG
|
A:CYS149
|
2.2
|
47.8
|
1.0
|
SG
|
A:CYS117
|
2.2
|
51.3
|
1.0
|
S1
|
A:FES3001
|
2.2
|
59.7
|
1.0
|
S2
|
A:FES3001
|
2.2
|
40.3
|
1.0
|
FE2
|
A:FES3001
|
3.1
|
55.0
|
1.0
|
CB
|
A:CYS149
|
3.7
|
50.5
|
1.0
|
CB
|
A:CYS117
|
3.7
|
60.1
|
1.0
|
CG2
|
A:THR152
|
4.1
|
65.5
|
1.0
|
N
|
A:CYS117
|
4.3
|
57.3
|
1.0
|
CB
|
A:CYS151
|
4.3
|
56.2
|
1.0
|
CA
|
A:CYS149
|
4.4
|
45.2
|
1.0
|
SG
|
A:CYS114
|
4.4
|
63.2
|
1.0
|
CA
|
A:CYS117
|
4.5
|
58.1
|
1.0
|
N
|
A:GLY115
|
4.6
|
59.9
|
1.0
|
N
|
A:CYS151
|
4.6
|
52.8
|
1.0
|
N
|
A:ARG150
|
4.7
|
49.3
|
1.0
|
OG1
|
A:THR152
|
4.7
|
62.0
|
1.0
|
N
|
A:THR152
|
4.7
|
62.1
|
1.0
|
N
|
A:THR118
|
4.8
|
61.0
|
1.0
|
OG1
|
A:THR118
|
4.9
|
65.2
|
1.0
|
C
|
A:CYS117
|
4.9
|
58.3
|
1.0
|
N
|
A:PHE116
|
4.9
|
50.2
|
1.0
|
C
|
A:CYS149
|
5.0
|
50.8
|
1.0
|
|
Iron binding site 2 out
of 4 in 6q6q
Go back to
Iron Binding Sites List in 6q6q
Iron binding site 2 out
of 4 in the Human Aldehyde Oxidase Snp G1269R
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 G1269R within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe3001
b:55.0
occ:1.00
|
FE2
|
A:FES3001
|
0.0
|
55.0
|
1.0
|
S1
|
A:FES3001
|
2.2
|
59.7
|
1.0
|
S2
|
A:FES3001
|
2.2
|
40.3
|
1.0
|
SG
|
A:CYS114
|
2.2
|
63.2
|
1.0
|
SG
|
A:CYS151
|
2.6
|
51.9
|
1.0
|
CB
|
A:CYS151
|
3.1
|
56.2
|
1.0
|
FE1
|
A:FES3001
|
3.1
|
58.8
|
1.0
|
CB
|
A:CYS114
|
3.1
|
53.5
|
1.0
|
N
|
A:CYS114
|
3.8
|
54.0
|
1.0
|
N
|
A:CYS151
|
3.9
|
52.8
|
1.0
|
CA
|
A:CYS114
|
4.0
|
49.4
|
1.0
|
CA
|
A:CYS151
|
4.1
|
62.8
|
1.0
|
N
|
A:GLY115
|
4.2
|
59.9
|
1.0
|
SG
|
A:CYS149
|
4.3
|
47.8
|
1.0
|
C
|
A:CYS114
|
4.5
|
54.9
|
1.0
|
N
|
A:ARG150
|
4.6
|
49.3
|
1.0
|
C
|
A:ARG150
|
4.7
|
52.6
|
1.0
|
N
|
A:PHE116
|
4.8
|
50.2
|
1.0
|
SG
|
A:CYS117
|
4.8
|
51.3
|
1.0
|
CG
|
A:MET753
|
4.9
|
55.2
|
1.0
|
CB
|
A:GLN113
|
5.0
|
57.6
|
1.0
|
|
Iron binding site 3 out
of 4 in 6q6q
Go back to
Iron Binding Sites List in 6q6q
Iron binding site 3 out
of 4 in the Human Aldehyde Oxidase Snp G1269R
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 G1269R within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe3002
b:79.7
occ:1.00
|
FE1
|
A:FES3002
|
0.0
|
79.7
|
1.0
|
S1
|
A:FES3002
|
2.2
|
66.7
|
1.0
|
S2
|
A:FES3002
|
2.2
|
71.0
|
1.0
|
SG
|
A:CYS49
|
2.3
|
65.5
|
1.0
|
N
|
A:CYS44
|
2.7
|
60.4
|
1.0
|
SG
|
A:CYS44
|
2.7
|
72.7
|
1.0
|
FE2
|
A:FES3002
|
3.1
|
72.5
|
1.0
|
CB
|
A:CYS49
|
3.3
|
60.9
|
1.0
|
N
|
A:GLY45
|
3.4
|
70.6
|
1.0
|
CA
|
A:CYS44
|
3.4
|
67.6
|
1.0
|
CB
|
A:CYS44
|
3.5
|
68.3
|
1.0
|
C
|
A:GLY43
|
3.6
|
60.2
|
1.0
|
CA
|
A:GLY43
|
3.8
|
61.1
|
1.0
|
C
|
A:CYS44
|
3.8
|
72.0
|
1.0
|
N
|
A:CYS49
|
3.9
|
60.1
|
1.0
|
N
|
A:GLY43
|
3.9
|
64.2
|
1.0
|
CA
|
A:CYS49
|
4.1
|
60.1
|
1.0
|
N
|
A:GLY50
|
4.3
|
55.5
|
1.0
|
N
|
A:GLY47
|
4.3
|
72.4
|
1.0
|
N
|
A:GLY48
|
4.5
|
70.5
|
1.0
|
CA
|
A:GLY45
|
4.5
|
71.7
|
1.0
|
N
|
A:GLY46
|
4.5
|
85.9
|
1.0
|
C
|
A:CYS49
|
4.6
|
58.4
|
1.0
|
SG
|
A:CYS74
|
4.6
|
52.6
|
1.0
|
N
|
A:ALA51
|
4.7
|
54.0
|
1.0
|
CA
|
A:GLY47
|
4.7
|
68.6
|
1.0
|
O
|
A:GLY43
|
4.8
|
63.5
|
1.0
|
C
|
A:GLY47
|
5.0
|
70.3
|
1.0
|
O
|
A:CYS44
|
5.0
|
76.8
|
1.0
|
|
Iron binding site 4 out
of 4 in 6q6q
Go back to
Iron Binding Sites List in 6q6q
Iron binding site 4 out
of 4 in the Human Aldehyde Oxidase Snp G1269R
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 G1269R within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe3002
b:72.5
occ:1.00
|
FE2
|
A:FES3002
|
0.0
|
72.5
|
1.0
|
S2
|
A:FES3002
|
2.2
|
71.0
|
1.0
|
S1
|
A:FES3002
|
2.2
|
66.7
|
1.0
|
SG
|
A:CYS52
|
2.3
|
53.5
|
1.0
|
SG
|
A:CYS74
|
2.3
|
52.6
|
1.0
|
FE1
|
A:FES3002
|
3.1
|
79.7
|
1.0
|
CB
|
A:CYS74
|
3.5
|
54.2
|
1.0
|
CB
|
A:CYS52
|
3.7
|
53.9
|
1.0
|
CB
|
A:ASN72
|
4.0
|
62.9
|
1.0
|
CA
|
A:GLY47
|
4.1
|
68.6
|
1.0
|
N
|
A:GLY47
|
4.2
|
72.4
|
1.0
|
N
|
A:CYS52
|
4.3
|
53.1
|
1.0
|
N
|
A:CYS74
|
4.3
|
54.5
|
1.0
|
ND2
|
A:ASN72
|
4.4
|
68.0
|
1.0
|
SG
|
A:CYS49
|
4.5
|
65.5
|
1.0
|
CG
|
A:ASN72
|
4.5
|
70.8
|
1.0
|
CA
|
A:CYS74
|
4.5
|
52.9
|
1.0
|
CA
|
A:CYS52
|
4.6
|
45.5
|
1.0
|
N
|
A:GLY45
|
4.7
|
70.6
|
1.0
|
CA
|
A:ASN72
|
4.8
|
58.0
|
1.0
|
N
|
A:GLY50
|
4.8
|
55.5
|
1.0
|
C
|
A:GLY47
|
4.9
|
70.3
|
1.0
|
N
|
A:ALA51
|
5.0
|
54.0
|
1.0
|
C
|
A:ASN72
|
5.0
|
61.1
|
1.0
|
|
Reference:
C.Mota,
M.Esmaeeli,
C.Coelho,
T.Santos-Silva,
M.Wolff,
A.Foti,
S.Leimkuhler,
M.J.Romao.
Human Aldehyde Oxidase (HAOX1): Structure Determination of the Moco-Free Form of the Natural Variant G1269R and Biophysical Studies of Single Nucleotide Polymorphisms. Febs Open Bio V. 9 925 2019.
ISSN: ESSN 2211-5463
PubMed: 30985987
DOI: 10.1002/2211-5463.12617
Page generated: Wed Aug 7 06:55:38 2024
|