Iron in PDB 8foc: Cryo-Em Structure of S. Cerevisiae Dna Polymerase Alpha-Primase in Apo State Conformation I
Iron Binding Sites:
The binding sites of Iron atom in the Cryo-Em Structure of S. Cerevisiae Dna Polymerase Alpha-Primase in Apo State Conformation I
(pdb code 8foc). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Cryo-Em Structure of S. Cerevisiae Dna Polymerase Alpha-Primase in Apo State Conformation I, PDB code: 8foc:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 8foc
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Iron Binding Sites List in 8foc
Iron binding site 1 out
of 4 in the Cryo-Em Structure of S. Cerevisiae Dna Polymerase Alpha-Primase in Apo State Conformation I
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Cryo-Em Structure of S. Cerevisiae Dna Polymerase Alpha-Primase in Apo State Conformation I within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:86.1
occ:1.00
|
FE1
|
B:SF4601
|
0.0
|
86.1
|
1.0
|
S2
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
S4
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
S3
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
FE3
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
FE2
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
FE4
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
CB
|
B:CYS336
|
3.1
|
11.0
|
1.0
|
S1
|
B:SF4601
|
3.9
|
86.1
|
1.0
|
N
|
B:CYS336
|
4.0
|
11.0
|
1.0
|
CG
|
B:PRO334
|
4.0
|
10.8
|
1.0
|
CB
|
B:PRO334
|
4.1
|
10.8
|
1.0
|
CA
|
B:CYS336
|
4.1
|
11.0
|
1.0
|
CG
|
B:PRO500
|
4.5
|
9.2
|
1.0
|
CD
|
B:PRO435
|
4.9
|
11.3
|
1.0
|
CD1
|
B:ILE420
|
5.0
|
8.1
|
1.0
|
|
Iron binding site 2 out
of 4 in 8foc
Go back to
Iron Binding Sites List in 8foc
Iron binding site 2 out
of 4 in the Cryo-Em Structure of S. Cerevisiae Dna Polymerase Alpha-Primase in Apo State Conformation I
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Cryo-Em Structure of S. Cerevisiae Dna Polymerase Alpha-Primase in Apo State Conformation I within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:86.1
occ:1.00
|
FE2
|
B:SF4601
|
0.0
|
86.1
|
1.0
|
S3
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
S1
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
S4
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
FE3
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
FE4
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
FE1
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
CB
|
B:CYS434
|
3.4
|
10.7
|
1.0
|
S2
|
B:SF4601
|
3.9
|
86.1
|
1.0
|
CA
|
B:CYS434
|
4.0
|
10.7
|
1.0
|
CD
|
B:PRO435
|
4.2
|
11.3
|
1.0
|
CB
|
B:CYS336
|
4.5
|
11.0
|
1.0
|
C
|
B:CYS434
|
4.6
|
10.7
|
1.0
|
N
|
B:PRO435
|
4.6
|
11.3
|
1.0
|
SG
|
B:CYS474
|
4.8
|
12.6
|
1.0
|
CB
|
B:CYS474
|
4.9
|
12.6
|
1.0
|
|
Iron binding site 3 out
of 4 in 8foc
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Iron Binding Sites List in 8foc
Iron binding site 3 out
of 4 in the Cryo-Em Structure of S. Cerevisiae Dna Polymerase Alpha-Primase in Apo State Conformation I
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Cryo-Em Structure of S. Cerevisiae Dna Polymerase Alpha-Primase in Apo State Conformation I within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:86.1
occ:1.00
|
FE3
|
B:SF4601
|
0.0
|
86.1
|
1.0
|
S2
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
S1
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
S4
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
FE4
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
FE2
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
FE1
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
CB
|
B:CYS417
|
3.6
|
9.5
|
1.0
|
S3
|
B:SF4601
|
3.9
|
86.1
|
1.0
|
CA
|
B:CYS417
|
4.2
|
9.5
|
1.0
|
SG
|
B:CYS474
|
4.4
|
12.6
|
1.0
|
CG
|
B:PRO500
|
4.8
|
9.2
|
1.0
|
CB
|
B:CYS474
|
4.8
|
12.6
|
1.0
|
CD
|
B:PRO500
|
5.0
|
9.2
|
1.0
|
|
Iron binding site 4 out
of 4 in 8foc
Go back to
Iron Binding Sites List in 8foc
Iron binding site 4 out
of 4 in the Cryo-Em Structure of S. Cerevisiae Dna Polymerase Alpha-Primase in Apo State Conformation I
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Cryo-Em Structure of S. Cerevisiae Dna Polymerase Alpha-Primase in Apo State Conformation I within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:86.1
occ:1.00
|
FE4
|
B:SF4601
|
0.0
|
86.1
|
1.0
|
S1
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
S3
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
S2
|
B:SF4601
|
2.3
|
86.1
|
1.0
|
SG
|
B:CYS474
|
2.4
|
12.6
|
1.0
|
FE3
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
FE2
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
FE1
|
B:SF4601
|
2.7
|
86.1
|
1.0
|
CB
|
B:CYS474
|
3.2
|
12.6
|
1.0
|
S4
|
B:SF4601
|
3.9
|
86.1
|
1.0
|
CB
|
B:PRO334
|
4.0
|
10.8
|
1.0
|
CA
|
B:CYS474
|
4.4
|
12.6
|
1.0
|
CG
|
B:PRO334
|
4.8
|
10.8
|
1.0
|
N
|
B:LEU335
|
5.0
|
11.2
|
1.0
|
|
Reference:
Z.Yuan,
R.Georgescu,
H.Li,
M.E.O'donnell.
Molecular Choreography of Primer Synthesis By the Eukaryotic Pol Alpha-Primase. Biorxiv 2023.
ISSN: ISSN 2692-8205
PubMed: 37205351
DOI: 10.1101/2023.05.03.539257
Page generated: Sat Aug 10 04:27:04 2024
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