Iron in PDB 7lvz: Crystal Structure of Ado
Enzymatic activity of Crystal Structure of Ado
All present enzymatic activity of Crystal Structure of Ado:
1.13.11.19;
Protein crystallography data
The structure of Crystal Structure of Ado, PDB code: 7lvz
was solved by
C.A.Bingman,
R.L.Fernandez,
R.W.Smith,
B.G.Fox,
T.C.Brunold,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
39.17 /
1.89
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
54.296,
139.525,
142.007,
90,
90,
90
|
R / Rfree (%)
|
19.1 /
22.8
|
Other elements in 7lvz:
The structure of Crystal Structure of Ado also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Ado
(pdb code 7lvz). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Crystal Structure of Ado, PDB code: 7lvz:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 7lvz
Go back to
Iron Binding Sites List in 7lvz
Iron binding site 1 out
of 4 in the Crystal Structure of Ado
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure of Ado within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe301
b:30.4
occ:1.00
|
O
|
A:HOH518
|
2.2
|
30.8
|
1.0
|
O
|
A:HOH465
|
2.2
|
28.6
|
1.0
|
NE2
|
A:HIS102
|
2.3
|
24.8
|
1.0
|
NE2
|
A:HIS100
|
2.3
|
29.4
|
1.0
|
O
|
A:HOH454
|
2.3
|
33.5
|
1.0
|
NE2
|
A:HIS179
|
2.4
|
27.8
|
1.0
|
CE1
|
A:HIS100
|
3.2
|
30.4
|
1.0
|
CD2
|
A:HIS102
|
3.2
|
30.1
|
1.0
|
CE1
|
A:HIS102
|
3.2
|
26.6
|
1.0
|
CD2
|
A:HIS100
|
3.3
|
25.5
|
1.0
|
CE1
|
A:HIS179
|
3.3
|
29.9
|
1.0
|
CD2
|
A:HIS179
|
3.3
|
28.7
|
1.0
|
HE1
|
A:HIS100
|
3.3
|
36.5
|
1.0
|
HD2
|
A:HIS102
|
3.4
|
36.2
|
1.0
|
HE1
|
A:HIS102
|
3.4
|
31.9
|
1.0
|
HD2
|
A:HIS100
|
3.4
|
30.6
|
1.0
|
HD2
|
A:HIS179
|
3.5
|
34.5
|
1.0
|
HE1
|
A:HIS179
|
3.5
|
35.9
|
1.0
|
O
|
A:HOH431
|
4.0
|
34.7
|
1.0
|
HD11
|
A:ILE181
|
4.1
|
37.5
|
1.0
|
HD22
|
A:LEU194
|
4.2
|
43.5
|
1.0
|
OH
|
A:TYR198
|
4.3
|
32.2
|
1.0
|
ND1
|
A:HIS100
|
4.3
|
29.3
|
1.0
|
ND1
|
A:HIS102
|
4.4
|
30.2
|
1.0
|
CG
|
A:HIS100
|
4.4
|
27.8
|
1.0
|
CG
|
A:HIS102
|
4.4
|
29.5
|
1.0
|
O
|
A:HOH506
|
4.4
|
35.5
|
1.0
|
ND1
|
A:HIS179
|
4.4
|
31.7
|
1.0
|
HD21
|
A:LEU171
|
4.4
|
39.8
|
1.0
|
CG
|
A:HIS179
|
4.5
|
29.3
|
1.0
|
OD2
|
A:ASP192
|
4.5
|
40.4
|
1.0
|
HH
|
A:TYR198
|
4.6
|
38.8
|
1.0
|
HD13
|
A:LEU194
|
4.7
|
43.0
|
1.0
|
HG23
|
A:ILE97
|
4.8
|
37.0
|
1.0
|
HD12
|
A:ILE181
|
4.8
|
37.5
|
1.0
|
CD1
|
A:ILE181
|
4.9
|
31.2
|
1.0
|
|
Iron binding site 2 out
of 4 in 7lvz
Go back to
Iron Binding Sites List in 7lvz
Iron binding site 2 out
of 4 in the Crystal Structure of Ado
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure of Ado within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe301
b:26.1
occ:1.00
|
O
|
B:HOH498
|
2.2
|
22.2
|
1.0
|
O
|
B:HOH441
|
2.2
|
22.7
|
1.0
|
NE2
|
B:HIS102
|
2.3
|
21.4
|
1.0
|
NE2
|
B:HIS100
|
2.3
|
22.3
|
1.0
|
O
|
B:HOH557
|
2.3
|
35.1
|
1.0
|
NE2
|
B:HIS179
|
2.5
|
25.6
|
1.0
|
CD2
|
B:HIS100
|
3.2
|
29.2
|
1.0
|
CE1
|
B:HIS102
|
3.2
|
24.2
|
1.0
|
CD2
|
B:HIS102
|
3.3
|
22.6
|
1.0
|
HD2
|
B:HIS100
|
3.3
|
35.1
|
1.0
|
CE1
|
B:HIS100
|
3.3
|
23.0
|
1.0
|
CE1
|
B:HIS179
|
3.3
|
25.2
|
1.0
|
HE1
|
B:HIS102
|
3.4
|
29.1
|
1.0
|
CD2
|
B:HIS179
|
3.4
|
27.8
|
1.0
|
HD2
|
B:HIS102
|
3.4
|
27.2
|
1.0
|
HE1
|
B:HIS179
|
3.5
|
30.3
|
1.0
|
HE1
|
B:HIS100
|
3.5
|
27.7
|
1.0
|
HD2
|
B:HIS179
|
3.6
|
33.4
|
1.0
|
O
|
B:HOH434
|
3.9
|
32.7
|
1.0
|
HD12
|
B:ILE181
|
4.1
|
41.1
|
1.0
|
OH
|
B:TYR198
|
4.3
|
29.2
|
1.0
|
HD23
|
B:LEU194
|
4.3
|
37.7
|
1.0
|
ND1
|
B:HIS102
|
4.4
|
26.4
|
1.0
|
CG
|
B:HIS100
|
4.4
|
23.9
|
1.0
|
ND1
|
B:HIS100
|
4.4
|
25.6
|
1.0
|
ND1
|
B:HIS179
|
4.4
|
29.6
|
1.0
|
CG
|
B:HIS102
|
4.4
|
26.5
|
1.0
|
OD2
|
B:ASP192
|
4.4
|
39.8
|
1.0
|
CG
|
B:HIS179
|
4.5
|
24.6
|
1.0
|
O
|
B:HOH506
|
4.5
|
33.2
|
1.0
|
HH
|
B:TYR198
|
4.6
|
35.1
|
1.0
|
HD11
|
B:LEU194
|
4.6
|
44.0
|
1.0
|
HD22
|
B:LEU171
|
4.6
|
37.1
|
1.0
|
HD13
|
B:ILE181
|
4.7
|
41.1
|
1.0
|
HG21
|
B:ILE97
|
4.8
|
38.0
|
1.0
|
CD1
|
B:ILE181
|
4.9
|
34.2
|
1.0
|
|
Iron binding site 3 out
of 4 in 7lvz
Go back to
Iron Binding Sites List in 7lvz
Iron binding site 3 out
of 4 in the Crystal Structure of Ado
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure of Ado within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe301
b:31.3
occ:1.00
|
O
|
B:HOH529
|
2.1
|
32.9
|
1.0
|
O
|
C:HOH460
|
2.2
|
31.1
|
1.0
|
NE2
|
C:HIS102
|
2.2
|
27.0
|
1.0
|
NE2
|
C:HIS100
|
2.3
|
29.5
|
1.0
|
NE2
|
C:HIS179
|
2.3
|
25.0
|
1.0
|
O
|
C:HOH485
|
2.4
|
35.4
|
1.0
|
CE1
|
C:HIS102
|
3.1
|
32.3
|
1.0
|
CD2
|
C:HIS102
|
3.2
|
30.4
|
1.0
|
CD2
|
C:HIS100
|
3.2
|
28.1
|
1.0
|
CE1
|
C:HIS179
|
3.3
|
30.8
|
1.0
|
CE1
|
C:HIS100
|
3.3
|
27.9
|
1.0
|
HE1
|
C:HIS102
|
3.3
|
38.9
|
1.0
|
HE2
|
B:HIS130
|
3.3
|
44.6
|
1.0
|
HD2
|
C:HIS100
|
3.3
|
33.8
|
1.0
|
CD2
|
C:HIS179
|
3.3
|
27.7
|
1.0
|
HD2
|
C:HIS102
|
3.3
|
36.5
|
1.0
|
HE1
|
C:HIS179
|
3.4
|
37.0
|
1.0
|
HE1
|
C:HIS100
|
3.5
|
33.6
|
1.0
|
HD2
|
C:HIS179
|
3.5
|
33.3
|
1.0
|
O
|
C:HOH427
|
4.1
|
34.2
|
1.0
|
NE2
|
B:HIS130
|
4.1
|
37.5
|
1.0
|
HD22
|
C:LEU194
|
4.2
|
45.3
|
1.0
|
ND1
|
C:HIS102
|
4.3
|
28.7
|
1.0
|
OH
|
C:TYR198
|
4.3
|
30.3
|
1.0
|
CG
|
C:HIS102
|
4.3
|
33.2
|
1.0
|
HD11
|
C:ILE181
|
4.3
|
39.1
|
1.0
|
HD22
|
C:LEU171
|
4.4
|
38.8
|
1.0
|
ND1
|
C:HIS179
|
4.4
|
32.8
|
1.0
|
CG
|
C:HIS100
|
4.4
|
26.2
|
1.0
|
ND1
|
C:HIS100
|
4.4
|
29.2
|
1.0
|
CG
|
C:HIS179
|
4.4
|
27.1
|
1.0
|
HH
|
C:TYR198
|
4.5
|
36.4
|
1.0
|
HD13
|
C:LEU194
|
4.5
|
50.7
|
1.0
|
O
|
C:HOH462
|
4.5
|
33.4
|
1.0
|
OD2
|
C:ASP192
|
4.5
|
38.2
|
1.0
|
HE1
|
B:HIS130
|
4.6
|
45.1
|
1.0
|
CE1
|
B:HIS130
|
4.8
|
37.9
|
1.0
|
HG21
|
C:ILE97
|
4.9
|
43.9
|
1.0
|
|
Iron binding site 4 out
of 4 in 7lvz
Go back to
Iron Binding Sites List in 7lvz
Iron binding site 4 out
of 4 in the Crystal Structure of Ado
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure of Ado within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe301
b:42.6
occ:1.00
|
NE2
|
D:HIS100
|
2.3
|
35.0
|
1.0
|
NE2
|
D:HIS102
|
2.3
|
33.7
|
1.0
|
O
|
D:HOH449
|
2.4
|
44.5
|
1.0
|
NE2
|
D:HIS179
|
2.4
|
29.9
|
1.0
|
O
|
D:HOH414
|
2.5
|
35.2
|
1.0
|
O
|
D:HOH491
|
2.6
|
46.7
|
1.0
|
CD2
|
D:HIS100
|
3.2
|
31.9
|
1.0
|
CE1
|
D:HIS102
|
3.2
|
31.7
|
1.0
|
CE1
|
D:HIS100
|
3.3
|
35.9
|
1.0
|
CE1
|
D:HIS179
|
3.3
|
34.9
|
1.0
|
CD2
|
D:HIS102
|
3.3
|
33.6
|
1.0
|
HD2
|
D:HIS100
|
3.3
|
38.4
|
1.0
|
HE1
|
D:HIS102
|
3.4
|
38.1
|
1.0
|
CD2
|
D:HIS179
|
3.4
|
33.5
|
1.0
|
HE2
|
A:HIS130
|
3.4
|
53.5
|
1.0
|
HE1
|
D:HIS179
|
3.5
|
42.0
|
1.0
|
HE1
|
D:HIS100
|
3.5
|
43.2
|
1.0
|
HD2
|
D:HIS179
|
3.5
|
40.3
|
1.0
|
HD2
|
D:HIS102
|
3.5
|
40.4
|
1.0
|
O
|
D:HOH410
|
4.0
|
37.8
|
1.0
|
HD11
|
D:ILE181
|
4.2
|
58.3
|
1.0
|
HD23
|
D:LEU194
|
4.2
|
51.7
|
1.0
|
NE2
|
A:HIS130
|
4.2
|
44.8
|
1.0
|
OH
|
D:TYR198
|
4.3
|
34.0
|
1.0
|
OD2
|
D:ASP192
|
4.4
|
52.2
|
1.0
|
ND1
|
D:HIS102
|
4.4
|
32.8
|
1.0
|
CG
|
D:HIS100
|
4.4
|
36.6
|
1.0
|
ND1
|
D:HIS100
|
4.4
|
39.8
|
1.0
|
ND1
|
D:HIS179
|
4.4
|
35.3
|
1.0
|
HD11
|
D:LEU194
|
4.4
|
48.2
|
1.0
|
CG
|
D:HIS102
|
4.5
|
32.8
|
1.0
|
HD23
|
D:LEU171
|
4.5
|
41.5
|
1.0
|
CG
|
D:HIS179
|
4.5
|
35.3
|
1.0
|
O
|
D:HOH422
|
4.6
|
39.8
|
1.0
|
HH
|
D:TYR198
|
4.6
|
40.5
|
1.0
|
HD12
|
D:ILE181
|
4.7
|
58.3
|
1.0
|
HE1
|
A:HIS130
|
4.7
|
54.3
|
1.0
|
HG22
|
D:ILE97
|
4.8
|
53.5
|
1.0
|
CE1
|
A:HIS130
|
4.9
|
45.5
|
1.0
|
CD1
|
D:ILE181
|
4.9
|
48.5
|
1.0
|
HE2
|
D:TYR198
|
4.9
|
41.8
|
1.0
|
|
Reference:
R.L.Fernandez,
L.D.Elmendorf,
R.W.Smith,
C.A.Bingman,
B.G.Fox,
T.C.Brunold.
The Crystal Structure of Cysteamine Dioxygenase Reveals the Origin of the Large Substrate Scope of This Vital Mammalian Enzyme. Biochemistry V. 60 3728 2021.
ISSN: ISSN 0006-2960
PubMed: 34762398
DOI: 10.1021/ACS.BIOCHEM.1C00463
Page generated: Thu Aug 8 08:02:56 2024
|