Zinc in PDB 8g99: Partial Auto-Inhibitory Complex of Xenopus Laevis Dna Polymerase Alpha-Primase
Enzymatic activity of Partial Auto-Inhibitory Complex of Xenopus Laevis Dna Polymerase Alpha-Primase
All present enzymatic activity of Partial Auto-Inhibitory Complex of Xenopus Laevis Dna Polymerase Alpha-Primase:
2.7.7.7;
Other elements in 8g99:
The structure of Partial Auto-Inhibitory Complex of Xenopus Laevis Dna Polymerase Alpha-Primase also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Partial Auto-Inhibitory Complex of Xenopus Laevis Dna Polymerase Alpha-Primase
(pdb code 8g99). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Partial Auto-Inhibitory Complex of Xenopus Laevis Dna Polymerase Alpha-Primase, PDB code: 8g99:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 8g99
Go back to
Zinc Binding Sites List in 8g99
Zinc binding site 1 out
of 2 in the Partial Auto-Inhibitory Complex of Xenopus Laevis Dna Polymerase Alpha-Primase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Partial Auto-Inhibitory Complex of Xenopus Laevis Dna Polymerase Alpha-Primase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1500
b:103.0
occ:1.00
|
SG
|
A:CYS1283
|
2.2
|
63.5
|
1.0
|
SG
|
A:CYS1312
|
2.3
|
90.9
|
1.0
|
SG
|
A:CYS1307
|
2.3
|
75.1
|
1.0
|
SG
|
A:CYS1280
|
2.3
|
79.9
|
1.0
|
HB2
|
A:CYS1280
|
2.9
|
64.6
|
1.0
|
HB3
|
A:CYS1280
|
2.9
|
65.1
|
1.0
|
CB
|
A:CYS1280
|
3.0
|
65.9
|
1.0
|
HB2
|
A:CYS1307
|
3.1
|
61.5
|
1.0
|
HB3
|
A:CYS1312
|
3.2
|
74.3
|
1.0
|
CB
|
A:CYS1312
|
3.2
|
76.5
|
1.0
|
CB
|
A:CYS1307
|
3.2
|
59.7
|
1.0
|
H
|
A:CYS1283
|
3.3
|
63.3
|
1.0
|
HB2
|
A:CYS1312
|
3.3
|
74.7
|
1.0
|
HB3
|
A:CYS1283
|
3.4
|
63.2
|
1.0
|
HB3
|
A:ALA1314
|
3.4
|
67.8
|
1.0
|
HB3
|
A:CYS1307
|
3.4
|
61.0
|
1.0
|
CB
|
A:CYS1283
|
3.5
|
63.2
|
1.0
|
HG22
|
A:THR1285
|
3.6
|
60.8
|
1.0
|
HG21
|
A:THR1285
|
4.0
|
60.5
|
1.0
|
HB3
|
A:LYS1309
|
4.0
|
69.4
|
1.0
|
HB3
|
A:LYS1282
|
4.0
|
67.2
|
1.0
|
N
|
A:CYS1283
|
4.0
|
59.5
|
1.0
|
HB2
|
A:CYS1283
|
4.2
|
63.0
|
1.0
|
CG2
|
A:THR1285
|
4.2
|
62.3
|
1.0
|
CB
|
A:ALA1314
|
4.3
|
67.7
|
1.0
|
H
|
A:THR1285
|
4.3
|
61.0
|
1.0
|
CA
|
A:CYS1283
|
4.3
|
61.5
|
1.0
|
H
|
A:ALA1314
|
4.4
|
69.1
|
1.0
|
CA
|
A:CYS1280
|
4.5
|
63.9
|
1.0
|
H
|
A:LYS1309
|
4.5
|
69.2
|
1.0
|
HD21
|
A:ASN1287
|
4.5
|
54.2
|
1.0
|
H
|
A:GLY1284
|
4.5
|
62.5
|
1.0
|
HB2
|
A:ALA1314
|
4.6
|
68.2
|
1.0
|
CA
|
A:CYS1307
|
4.6
|
54.5
|
1.0
|
CA
|
A:CYS1312
|
4.6
|
73.3
|
1.0
|
HB2
|
A:LYS1309
|
4.7
|
69.5
|
1.0
|
H
|
A:LYS1282
|
4.7
|
67.3
|
1.0
|
HA
|
A:CYS1280
|
4.7
|
64.1
|
1.0
|
HA
|
A:CYS1307
|
4.8
|
61.0
|
1.0
|
CB
|
A:LYS1309
|
4.8
|
70.2
|
1.0
|
HD3
|
A:LYS1309
|
4.8
|
69.5
|
1.0
|
HB1
|
A:ALA1314
|
4.8
|
67.9
|
1.0
|
HG23
|
A:THR1285
|
4.8
|
60.6
|
1.0
|
O
|
A:ALA1314
|
4.9
|
67.4
|
1.0
|
HA
|
A:CYS1312
|
5.0
|
74.8
|
1.0
|
N
|
A:GLY1284
|
5.0
|
61.0
|
1.0
|
CB
|
A:LYS1282
|
5.0
|
66.6
|
1.0
|
|
Zinc binding site 2 out
of 2 in 8g99
Go back to
Zinc Binding Sites List in 8g99
Zinc binding site 2 out
of 2 in the Partial Auto-Inhibitory Complex of Xenopus Laevis Dna Polymerase Alpha-Primase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Partial Auto-Inhibitory Complex of Xenopus Laevis Dna Polymerase Alpha-Primase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1501
b:83.8
occ:1.00
|
SG
|
A:CYS1371
|
2.3
|
49.4
|
1.0
|
SG
|
A:CYS1368
|
2.3
|
43.0
|
1.0
|
SG
|
A:CYS1350
|
2.3
|
35.9
|
1.0
|
SG
|
A:CYS1345
|
2.3
|
46.6
|
1.0
|
HB3
|
A:CYS1368
|
2.9
|
33.9
|
1.0
|
HB2
|
A:CYS1345
|
3.0
|
35.8
|
1.0
|
CB
|
A:CYS1368
|
3.1
|
34.7
|
1.0
|
HB3
|
A:CYS1350
|
3.1
|
40.6
|
1.0
|
CB
|
A:CYS1345
|
3.2
|
30.9
|
1.0
|
H
|
A:CYS1371
|
3.2
|
40.5
|
1.0
|
CB
|
A:CYS1350
|
3.2
|
39.5
|
1.0
|
HB2
|
A:CYS1368
|
3.3
|
34.0
|
1.0
|
HB2
|
A:CYS1350
|
3.4
|
40.8
|
1.0
|
HB3
|
A:CYS1345
|
3.5
|
35.1
|
1.0
|
HB3
|
A:ALA1370
|
3.5
|
35.1
|
1.0
|
HB3
|
A:ALA1374
|
3.5
|
36.8
|
1.0
|
HB3
|
A:CYS1371
|
3.5
|
41.5
|
1.0
|
CB
|
A:CYS1371
|
3.5
|
43.0
|
1.0
|
HB3
|
A:ASN1352
|
3.8
|
36.5
|
1.0
|
N
|
A:CYS1371
|
3.9
|
36.5
|
1.0
|
H
|
A:ASN1352
|
4.0
|
37.9
|
1.0
|
HB2
|
A:ASN1352
|
4.0
|
36.9
|
1.0
|
HB3
|
A:GLU1347
|
4.1
|
42.1
|
1.0
|
HB2
|
A:CYS1371
|
4.3
|
41.2
|
1.0
|
H
|
A:ALA1370
|
4.3
|
35.3
|
1.0
|
CA
|
A:CYS1371
|
4.3
|
38.1
|
1.0
|
CB
|
A:ASN1352
|
4.4
|
34.1
|
1.0
|
CB
|
A:ALA1370
|
4.4
|
31.9
|
1.0
|
CB
|
A:ALA1374
|
4.5
|
39.1
|
1.0
|
CA
|
A:CYS1368
|
4.5
|
31.3
|
1.0
|
H
|
A:SER1372
|
4.6
|
38.3
|
1.0
|
CA
|
A:CYS1345
|
4.6
|
23.4
|
1.0
|
CA
|
A:CYS1350
|
4.6
|
41.4
|
1.0
|
HA
|
A:CYS1345
|
4.7
|
34.5
|
1.0
|
H
|
A:ALA1374
|
4.7
|
36.3
|
1.0
|
HB1
|
A:ALA1374
|
4.8
|
36.6
|
1.0
|
H
|
A:GLN1351
|
4.8
|
41.6
|
1.0
|
C
|
A:ALA1370
|
4.8
|
34.7
|
1.0
|
N
|
A:ASN1352
|
4.8
|
34.3
|
1.0
|
H
|
A:GLU1347
|
4.8
|
42.3
|
1.0
|
C
|
A:CYS1368
|
4.8
|
28.4
|
1.0
|
HB1
|
A:ALA1370
|
4.9
|
35.4
|
1.0
|
H
|
A:LYS1373
|
4.9
|
39.9
|
1.0
|
O
|
A:CYS1368
|
4.9
|
38.7
|
1.0
|
N
|
A:ALA1370
|
4.9
|
36.0
|
1.0
|
HB2
|
A:ALA1374
|
4.9
|
36.2
|
1.0
|
CB
|
A:GLU1347
|
4.9
|
39.3
|
1.0
|
HB2
|
A:GLU1347
|
5.0
|
42.1
|
1.0
|
HB2
|
A:ALA1370
|
5.0
|
35.0
|
1.0
|
CA
|
A:ALA1370
|
5.0
|
32.3
|
1.0
|
C
|
A:CYS1350
|
5.0
|
40.8
|
1.0
|
HA
|
A:CYS1368
|
5.0
|
33.8
|
1.0
|
N
|
A:GLN1351
|
5.0
|
39.1
|
1.0
|
|
Reference:
E.A.Mullins,
L.E.Salay,
C.L.Durie,
J.E.Jackman,
M.D.Ohi,
W.J.Chazin,
B.F.Eichman.
A Mechanistic Model of Primer Synthesis From Catalytic Structures of Dna Polymerase Alpha-Primase. Biorxiv 2023.
ISSN: ISSN 2692-8205
PubMed: 36993335
DOI: 10.1101/2023.03.16.533013
Page generated: Wed Oct 30 20:47:44 2024
|