Iron in PDB 7lc7: Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima
Enzymatic activity of Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima
All present enzymatic activity of Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima:
1.17.99.6;
Protein crystallography data
The structure of Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima, PDB code: 7lc7
was solved by
Q.Li,
S.D.Bruner,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.53 /
1.58
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
53.335,
104.783,
73.741,
90,
90,
90
|
R / Rfree (%)
|
20 /
24.3
|
Other elements in 7lc7:
The structure of Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima
(pdb code 7lc7). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 5 binding sites of Iron where determined in the
Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima, PDB code: 7lc7:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
Iron binding site 1 out
of 5 in 7lc7
Go back to
Iron Binding Sites List in 7lc7
Iron binding site 1 out
of 5 in the Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima
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 Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe301
b:29.9
occ:1.00
|
FE1
|
A:SF4301
|
0.0
|
29.9
|
1.0
|
S2
|
A:SF4301
|
2.3
|
25.8
|
1.0
|
S4
|
A:SF4301
|
2.3
|
27.7
|
1.0
|
S3
|
A:SF4301
|
2.3
|
33.4
|
1.0
|
SG
|
A:CYS169
|
2.5
|
34.3
|
1.0
|
FE3
|
A:SF4301
|
2.6
|
27.1
|
1.0
|
FE2
|
A:SF4301
|
2.7
|
30.7
|
1.0
|
FE4
|
A:SF4301
|
2.7
|
31.9
|
1.0
|
CB
|
A:CYS169
|
3.2
|
30.9
|
1.0
|
S1
|
A:SF4301
|
3.8
|
29.7
|
1.0
|
O
|
A:HOH481
|
4.1
|
37.6
|
1.0
|
CA
|
A:CYS169
|
4.5
|
30.5
|
1.0
|
C
|
A:CYS169
|
4.5
|
29.8
|
1.0
|
OE1
|
A:GLU82
|
4.6
|
51.7
|
1.0
|
N
|
A:GLY170
|
4.7
|
27.2
|
1.0
|
CE
|
A:LYS120
|
4.8
|
39.6
|
1.0
|
SG
|
A:CYS171
|
4.8
|
34.1
|
1.0
|
SG
|
A:CYS87
|
4.9
|
33.2
|
1.0
|
SG
|
A:CYS90
|
4.9
|
23.8
|
1.0
|
O
|
A:CYS169
|
4.9
|
26.4
|
1.0
|
ND2
|
A:ASN32
|
4.9
|
25.2
|
1.0
|
|
Iron binding site 2 out
of 5 in 7lc7
Go back to
Iron Binding Sites List in 7lc7
Iron binding site 2 out
of 5 in the Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima
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 Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe301
b:30.7
occ:1.00
|
FE2
|
A:SF4301
|
0.0
|
30.7
|
1.0
|
S1
|
A:SF4301
|
2.3
|
29.7
|
1.0
|
S3
|
A:SF4301
|
2.3
|
33.4
|
1.0
|
S4
|
A:SF4301
|
2.3
|
27.7
|
1.0
|
SG
|
A:CYS87
|
2.5
|
33.2
|
1.0
|
FE3
|
A:SF4301
|
2.7
|
27.1
|
1.0
|
FE1
|
A:SF4301
|
2.7
|
29.9
|
1.0
|
FE4
|
A:SF4301
|
2.7
|
31.9
|
1.0
|
CB
|
A:CYS87
|
3.3
|
32.9
|
1.0
|
CA
|
A:CYS87
|
3.6
|
30.2
|
1.0
|
S2
|
A:SF4301
|
3.9
|
25.8
|
1.0
|
NH2
|
A:ARG86
|
4.0
|
46.1
|
1.0
|
NE
|
A:ARG86
|
4.0
|
42.2
|
1.0
|
N
|
A:CYS87
|
4.2
|
29.7
|
1.0
|
CZ
|
A:ARG86
|
4.5
|
44.9
|
1.0
|
CB
|
A:CYS90
|
4.7
|
25.2
|
1.0
|
SG
|
A:CYS90
|
4.8
|
23.8
|
1.0
|
C
|
A:ARG86
|
4.8
|
30.3
|
1.0
|
SG
|
A:CYS169
|
4.9
|
34.3
|
1.0
|
C
|
A:CYS87
|
4.9
|
29.6
|
1.0
|
O
|
A:ARG86
|
4.9
|
30.8
|
1.0
|
SG
|
A:CYS171
|
5.0
|
34.1
|
1.0
|
|
Iron binding site 3 out
of 5 in 7lc7
Go back to
Iron Binding Sites List in 7lc7
Iron binding site 3 out
of 5 in the Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima
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 Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe301
b:27.1
occ:1.00
|
FE3
|
A:SF4301
|
0.0
|
27.1
|
1.0
|
S2
|
A:SF4301
|
2.3
|
25.8
|
1.0
|
S1
|
A:SF4301
|
2.3
|
29.7
|
1.0
|
S4
|
A:SF4301
|
2.3
|
27.7
|
1.0
|
SG
|
A:CYS90
|
2.4
|
23.8
|
1.0
|
FE1
|
A:SF4301
|
2.6
|
29.9
|
1.0
|
FE4
|
A:SF4301
|
2.7
|
31.9
|
1.0
|
FE2
|
A:SF4301
|
2.7
|
30.7
|
1.0
|
CB
|
A:CYS90
|
3.1
|
25.2
|
1.0
|
S3
|
A:SF4301
|
3.8
|
33.4
|
1.0
|
O
|
A:HOH481
|
4.0
|
37.6
|
1.0
|
ND2
|
A:ASN32
|
4.3
|
25.2
|
1.0
|
CA
|
A:CYS90
|
4.6
|
22.0
|
1.0
|
CZ2
|
A:TRP70
|
4.6
|
30.7
|
1.0
|
CB
|
A:ASN32
|
4.7
|
24.3
|
1.0
|
CA
|
A:CYS87
|
4.7
|
30.2
|
1.0
|
SG
|
A:CYS171
|
4.8
|
34.1
|
1.0
|
NE1
|
A:TRP70
|
4.8
|
25.6
|
1.0
|
CG
|
A:ASN32
|
4.9
|
22.8
|
1.0
|
SG
|
A:CYS87
|
4.9
|
33.2
|
1.0
|
CB
|
A:CYS171
|
5.0
|
30.9
|
1.0
|
SG
|
A:CYS169
|
5.0
|
34.3
|
1.0
|
|
Iron binding site 4 out
of 5 in 7lc7
Go back to
Iron Binding Sites List in 7lc7
Iron binding site 4 out
of 5 in the Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima
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 Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe301
b:31.9
occ:1.00
|
FE4
|
A:SF4301
|
0.0
|
31.9
|
1.0
|
S1
|
A:SF4301
|
2.3
|
29.7
|
1.0
|
S3
|
A:SF4301
|
2.3
|
33.4
|
1.0
|
S2
|
A:SF4301
|
2.3
|
25.8
|
1.0
|
SG
|
A:CYS171
|
2.4
|
34.1
|
1.0
|
FE3
|
A:SF4301
|
2.7
|
27.1
|
1.0
|
FE1
|
A:SF4301
|
2.7
|
29.9
|
1.0
|
FE2
|
A:SF4301
|
2.7
|
30.7
|
1.0
|
CB
|
A:CYS171
|
3.3
|
30.9
|
1.0
|
S4
|
A:SF4301
|
3.9
|
27.7
|
1.0
|
NH2
|
A:ARG86
|
4.1
|
46.1
|
1.0
|
NE
|
A:ARG86
|
4.2
|
42.2
|
1.0
|
N
|
A:CYS171
|
4.2
|
27.5
|
1.0
|
CA
|
A:CYS171
|
4.4
|
30.0
|
1.0
|
CB
|
A:SER174
|
4.5
|
35.0
|
1.0
|
CZ
|
A:ARG86
|
4.5
|
44.9
|
1.0
|
OG
|
A:SER174
|
4.5
|
33.8
|
1.0
|
CZ2
|
A:TRP70
|
4.7
|
30.7
|
1.0
|
CB
|
A:CYS169
|
4.8
|
30.9
|
1.0
|
SG
|
A:CYS90
|
4.8
|
23.8
|
1.0
|
SG
|
A:CYS169
|
4.9
|
34.3
|
1.0
|
N
|
A:SER174
|
4.9
|
37.1
|
1.0
|
CD2
|
A:PHE173
|
5.0
|
39.8
|
1.0
|
|
Iron binding site 5 out
of 5 in 7lc7
Go back to
Iron Binding Sites List in 7lc7
Iron binding site 5 out
of 5 in the Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Gmp From Thermotoga Maritima within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe303
b:15.4
occ:1.00
|
OD2
|
A:ASP13
|
1.9
|
18.6
|
1.0
|
CL
|
A:CL304
|
2.2
|
28.2
|
1.0
|
SG
|
A:CYS9
|
2.3
|
16.6
|
1.0
|
SG
|
A:CYS10
|
2.3
|
16.6
|
1.0
|
CG
|
A:ASP13
|
2.9
|
20.8
|
1.0
|
CB
|
A:CYS9
|
3.2
|
15.8
|
1.0
|
CB
|
A:CYS10
|
3.4
|
16.2
|
1.0
|
CB
|
A:ASP13
|
3.4
|
15.1
|
1.0
|
N
|
A:CYS10
|
3.5
|
15.2
|
1.0
|
C
|
A:CYS9
|
3.9
|
17.0
|
1.0
|
CA
|
A:CYS10
|
4.0
|
13.6
|
1.0
|
OD1
|
A:ASP13
|
4.0
|
19.6
|
1.0
|
C8
|
A:5GP302
|
4.1
|
29.1
|
0.5
|
CA
|
A:CYS9
|
4.1
|
15.1
|
1.0
|
NE2
|
A:GLN166
|
4.2
|
27.2
|
1.0
|
N7
|
A:5GP302
|
4.3
|
28.7
|
0.5
|
N9
|
A:5GP302
|
4.4
|
32.5
|
0.5
|
O
|
A:CYS10
|
4.5
|
15.5
|
1.0
|
O
|
A:CYS9
|
4.6
|
16.7
|
1.0
|
N
|
A:ASP13
|
4.6
|
15.3
|
1.0
|
C
|
A:CYS10
|
4.6
|
16.2
|
1.0
|
CA
|
A:ASP13
|
4.6
|
13.7
|
1.0
|
C5
|
A:5GP302
|
4.7
|
28.4
|
0.5
|
O
|
A:HOH422
|
4.7
|
24.8
|
1.0
|
O
|
A:HOH470
|
4.7
|
34.2
|
1.0
|
C4
|
A:5GP302
|
4.7
|
31.2
|
0.5
|
N
|
A:CYS9
|
4.8
|
13.5
|
1.0
|
CD2
|
A:LEU114
|
4.8
|
19.5
|
1.0
|
CB
|
A:SER117
|
4.8
|
28.3
|
1.0
|
C1'
|
A:5GP302
|
4.9
|
33.5
|
0.5
|
OG1
|
A:THR113
|
4.9
|
14.3
|
1.0
|
|
Reference:
Q.Li,
S.D.Bruner.
The Epoxyqueuosine Reductase Queh in the Biosynthesis of Trna Queuosine Is A Unique Metalloenzyme To Be Published.
Page generated: Thu Aug 8 06:57:16 2024
|