Iron in PDB 6o9m: Structure of the Human Apo Tfiih
Enzymatic activity of Structure of the Human Apo Tfiih
All present enzymatic activity of Structure of the Human Apo Tfiih:
3.6.4.12;
Other elements in 6o9m:
The structure of Structure of the Human Apo Tfiih also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Structure of the Human Apo Tfiih
(pdb code 6o9m). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Structure of the Human Apo Tfiih, PDB code: 6o9m:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 6o9m
Go back to
Iron Binding Sites List in 6o9m
Iron binding site 1 out
of 4 in the Structure of the Human Apo Tfiih
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Structure of the Human Apo Tfiih within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
0:Fe801
b:0.0
occ:1.00
|
FE1
|
0:SF4801
|
0.0
|
0.0
|
1.0
|
S4
|
0:SF4801
|
2.1
|
0.0
|
1.0
|
S2
|
0:SF4801
|
2.1
|
0.0
|
1.0
|
S3
|
0:SF4801
|
2.2
|
0.0
|
1.0
|
SG
|
0:CYS116
|
2.2
|
0.2
|
1.0
|
FE3
|
0:SF4801
|
2.9
|
0.0
|
1.0
|
FE2
|
0:SF4801
|
2.9
|
0.0
|
1.0
|
CB
|
0:CYS116
|
3.0
|
0.5
|
1.0
|
FE4
|
0:SF4801
|
3.3
|
0.0
|
1.0
|
CA
|
0:CYS116
|
3.6
|
0.6
|
1.0
|
CD2
|
0:HIS118
|
3.7
|
0.2
|
1.0
|
S1
|
0:SF4801
|
3.8
|
0.0
|
1.0
|
SG
|
0:CYS134
|
4.2
|
0.2
|
1.0
|
NE2
|
0:HIS118
|
4.3
|
0.9
|
1.0
|
N
|
0:ILE117
|
4.5
|
1.0
|
1.0
|
C
|
0:CYS116
|
4.6
|
0.5
|
1.0
|
N
|
0:CYS116
|
4.6
|
0.9
|
1.0
|
CG
|
0:HIS118
|
4.7
|
0.3
|
1.0
|
O
|
0:LEU115
|
4.7
|
0.4
|
1.0
|
CB
|
0:CYS134
|
4.8
|
0.2
|
1.0
|
C
|
0:LEU115
|
5.0
|
0.8
|
1.0
|
CG1
|
0:VAL121
|
5.0
|
0.2
|
1.0
|
|
Iron binding site 2 out
of 4 in 6o9m
Go back to
Iron Binding Sites List in 6o9m
Iron binding site 2 out
of 4 in the Structure of the Human Apo Tfiih
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Structure of the Human Apo Tfiih within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
0:Fe801
b:0.0
occ:1.00
|
FE2
|
0:SF4801
|
0.0
|
0.0
|
1.0
|
S3
|
0:SF4801
|
2.1
|
0.0
|
1.0
|
S4
|
0:SF4801
|
2.2
|
0.0
|
1.0
|
S1
|
0:SF4801
|
2.2
|
0.0
|
1.0
|
SG
|
0:CYS155
|
2.3
|
0.7
|
1.0
|
FE1
|
0:SF4801
|
2.9
|
0.0
|
1.0
|
FE4
|
0:SF4801
|
3.0
|
0.0
|
1.0
|
FE3
|
0:SF4801
|
3.0
|
0.0
|
1.0
|
S2
|
0:SF4801
|
3.6
|
0.0
|
1.0
|
CB
|
0:CYS155
|
3.8
|
0.1
|
1.0
|
OG1
|
0:THR138
|
3.9
|
0.2
|
1.0
|
NH1
|
0:ARG299
|
4.0
|
0.0
|
1.0
|
NE2
|
0:HIS118
|
4.2
|
0.9
|
1.0
|
SG
|
0:CYS134
|
4.2
|
0.2
|
1.0
|
CD2
|
0:HIS118
|
4.3
|
0.2
|
1.0
|
CA
|
0:CYS155
|
4.5
|
0.6
|
1.0
|
SG
|
0:CYS190
|
4.7
|
0.0
|
1.0
|
SG
|
0:CYS116
|
4.9
|
0.2
|
1.0
|
|
Iron binding site 3 out
of 4 in 6o9m
Go back to
Iron Binding Sites List in 6o9m
Iron binding site 3 out
of 4 in the Structure of the Human Apo Tfiih
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Structure of the Human Apo Tfiih within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
0:Fe801
b:0.0
occ:1.00
|
FE3
|
0:SF4801
|
0.0
|
0.0
|
1.0
|
S1
|
0:SF4801
|
2.1
|
0.0
|
1.0
|
S4
|
0:SF4801
|
2.2
|
0.0
|
1.0
|
S2
|
0:SF4801
|
2.3
|
0.0
|
1.0
|
SG
|
0:CYS134
|
2.3
|
0.2
|
1.0
|
FE1
|
0:SF4801
|
2.9
|
0.0
|
1.0
|
FE4
|
0:SF4801
|
2.9
|
0.0
|
1.0
|
FE2
|
0:SF4801
|
3.0
|
0.0
|
1.0
|
NH1
|
0:ARG299
|
3.2
|
0.0
|
1.0
|
NH2
|
0:ARG299
|
3.5
|
0.0
|
1.0
|
S3
|
0:SF4801
|
3.6
|
0.0
|
1.0
|
CZ
|
0:ARG299
|
3.8
|
0.0
|
1.0
|
CB
|
0:CYS134
|
3.8
|
0.2
|
1.0
|
CD1
|
0:LEU115
|
4.2
|
0.6
|
1.0
|
CG
|
0:LEU115
|
4.3
|
0.8
|
1.0
|
CD2
|
0:LEU115
|
4.7
|
93.3
|
1.0
|
OG1
|
0:THR138
|
4.8
|
0.2
|
1.0
|
SG
|
0:CYS116
|
4.9
|
0.2
|
1.0
|
CA
|
0:CYS134
|
4.9
|
0.5
|
1.0
|
SG
|
0:CYS190
|
5.0
|
0.0
|
1.0
|
CB
|
0:CYS116
|
5.0
|
0.5
|
1.0
|
|
Iron binding site 4 out
of 4 in 6o9m
Go back to
Iron Binding Sites List in 6o9m
Iron binding site 4 out
of 4 in the Structure of the Human Apo Tfiih
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Structure of the Human Apo Tfiih within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
0:Fe801
b:0.0
occ:1.00
|
FE4
|
0:SF4801
|
0.0
|
0.0
|
1.0
|
S2
|
0:SF4801
|
2.1
|
0.0
|
1.0
|
S1
|
0:SF4801
|
2.1
|
0.0
|
1.0
|
SG
|
0:CYS190
|
2.2
|
0.0
|
1.0
|
S3
|
0:SF4801
|
2.2
|
0.0
|
1.0
|
FE3
|
0:SF4801
|
2.9
|
0.0
|
1.0
|
FE2
|
0:SF4801
|
3.0
|
0.0
|
1.0
|
FE1
|
0:SF4801
|
3.3
|
0.0
|
1.0
|
CB
|
0:CYS190
|
3.6
|
0.0
|
1.0
|
S4
|
0:SF4801
|
3.8
|
0.0
|
1.0
|
CE2
|
0:PHE157
|
4.1
|
0.4
|
1.0
|
CA
|
0:CYS190
|
4.4
|
0.0
|
1.0
|
CE2
|
0:PHE193
|
4.5
|
0.0
|
1.0
|
O
|
0:LEU115
|
4.5
|
0.4
|
1.0
|
CD2
|
0:PHE157
|
4.6
|
0.5
|
1.0
|
CD2
|
0:PHE193
|
4.7
|
0.0
|
1.0
|
SG
|
0:CYS155
|
4.8
|
0.7
|
1.0
|
CD
|
0:PRO191
|
4.8
|
0.0
|
1.0
|
CZ
|
0:PHE157
|
4.9
|
0.9
|
1.0
|
CD1
|
0:LEU115
|
4.9
|
0.6
|
1.0
|
NH1
|
0:ARG299
|
4.9
|
0.0
|
1.0
|
|
Reference:
C.Yan,
T.Dodd,
Y.He,
J.A.Tainer,
S.E.Tsutakawa,
I.Ivanov.
Transcription Preinitiation Complex Structure and Dynamics Provide Insight Into Genetic Diseases. Nat.Struct.Mol.Biol. V. 26 397 2019.
ISSN: ESSN 1545-9985
PubMed: 31110295
DOI: 10.1038/S41594-019-0220-3
Page generated: Wed Aug 7 04:13:01 2024
|