Zinc in PDB 5lgy: Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element.
Protein crystallography data
The structure of Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element., PDB code: 5lgy
was solved by
E.Arbely,
R.Vainer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
43.46 /
2.92
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
67.703,
70.344,
104.995,
90.00,
95.83,
90.00
|
R / Rfree (%)
|
23.8 /
27.7
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element.
(pdb code 5lgy). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element., PDB code: 5lgy:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 5lgy
Go back to
Zinc Binding Sites List in 5lgy
Zinc binding site 1 out
of 4 in the Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn401
b:37.5
occ:1.00
|
ND1
|
A:HIS179
|
2.1
|
35.1
|
1.0
|
SG
|
A:CYS238
|
2.4
|
45.3
|
1.0
|
SG
|
A:CYS242
|
2.4
|
38.8
|
1.0
|
SG
|
A:CYS176
|
2.5
|
45.3
|
1.0
|
CE1
|
A:HIS179
|
2.9
|
33.7
|
1.0
|
CG
|
A:HIS179
|
3.1
|
38.7
|
1.0
|
CB
|
A:CYS242
|
3.1
|
35.7
|
1.0
|
CB
|
A:CYS176
|
3.3
|
40.6
|
1.0
|
CB
|
A:CYS238
|
3.4
|
36.0
|
1.0
|
CB
|
A:HIS179
|
3.6
|
45.4
|
1.0
|
CA
|
A:CYS238
|
3.8
|
36.1
|
1.0
|
NE2
|
A:HIS179
|
3.9
|
37.3
|
1.0
|
N
|
A:CYS176
|
4.0
|
46.4
|
1.0
|
CD2
|
A:HIS179
|
4.1
|
39.0
|
1.0
|
CA
|
A:CYS176
|
4.3
|
41.6
|
1.0
|
N
|
A:ASN239
|
4.4
|
33.5
|
1.0
|
CA
|
A:CYS242
|
4.5
|
39.5
|
1.0
|
O
|
A:MET237
|
4.5
|
35.3
|
1.0
|
C
|
A:CYS238
|
4.6
|
37.5
|
1.0
|
N
|
A:HIS179
|
4.7
|
41.4
|
1.0
|
CA
|
A:HIS179
|
4.7
|
41.1
|
1.0
|
CE
|
B:MET243
|
4.8
|
37.0
|
1.0
|
O
|
A:CYS176
|
5.0
|
48.1
|
1.0
|
SD
|
B:MET243
|
5.0
|
50.6
|
1.0
|
O
|
A:ASN239
|
5.0
|
35.0
|
1.0
|
N
|
A:CYS238
|
5.0
|
37.9
|
1.0
|
|
Zinc binding site 2 out
of 4 in 5lgy
Go back to
Zinc Binding Sites List in 5lgy
Zinc binding site 2 out
of 4 in the Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn301
b:30.9
occ:1.00
|
ND1
|
B:HIS179
|
2.3
|
31.1
|
1.0
|
SG
|
B:CYS242
|
2.3
|
34.1
|
1.0
|
SG
|
B:CYS176
|
2.4
|
37.3
|
1.0
|
SG
|
B:CYS238
|
2.5
|
37.2
|
1.0
|
CB
|
B:CYS242
|
2.8
|
35.5
|
1.0
|
CE1
|
B:HIS179
|
3.0
|
28.8
|
1.0
|
CB
|
B:CYS176
|
3.1
|
36.6
|
1.0
|
CG
|
B:HIS179
|
3.3
|
32.1
|
1.0
|
CB
|
B:CYS238
|
3.7
|
32.4
|
1.0
|
CB
|
B:HIS179
|
3.8
|
31.7
|
1.0
|
N
|
B:CYS176
|
4.0
|
36.9
|
1.0
|
NE2
|
B:HIS179
|
4.0
|
33.1
|
1.0
|
CA
|
B:CYS242
|
4.1
|
37.1
|
1.0
|
CA
|
B:CYS176
|
4.2
|
34.9
|
1.0
|
CA
|
B:CYS238
|
4.2
|
29.3
|
1.0
|
CD2
|
B:HIS179
|
4.2
|
35.9
|
1.0
|
CE
|
A:MET243
|
4.5
|
42.6
|
1.0
|
N
|
B:ASN239
|
4.6
|
29.9
|
1.0
|
N
|
B:HIS179
|
4.7
|
38.0
|
1.0
|
C
|
B:CYS238
|
4.9
|
29.0
|
1.0
|
C
|
B:CYS242
|
4.9
|
43.3
|
1.0
|
CA
|
B:HIS179
|
4.9
|
34.2
|
1.0
|
SD
|
A:MET243
|
4.9
|
46.7
|
1.0
|
O
|
B:ASN239
|
4.9
|
34.7
|
1.0
|
C
|
B:CYS176
|
5.0
|
38.1
|
1.0
|
O
|
B:MET237
|
5.0
|
33.4
|
1.0
|
|
Zinc binding site 3 out
of 4 in 5lgy
Go back to
Zinc Binding Sites List in 5lgy
Zinc binding site 3 out
of 4 in the Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn301
b:34.7
occ:1.00
|
ND1
|
C:HIS179
|
2.1
|
42.2
|
1.0
|
SG
|
C:CYS238
|
2.3
|
33.0
|
1.0
|
SG
|
C:CYS242
|
2.4
|
47.9
|
1.0
|
SG
|
C:CYS176
|
2.4
|
44.6
|
1.0
|
CE1
|
C:HIS179
|
2.8
|
39.9
|
1.0
|
CG
|
C:HIS179
|
3.1
|
36.9
|
1.0
|
CB
|
C:CYS242
|
3.2
|
37.7
|
1.0
|
CB
|
C:CYS238
|
3.3
|
32.3
|
1.0
|
CB
|
C:CYS176
|
3.5
|
33.7
|
1.0
|
CB
|
C:HIS179
|
3.6
|
37.8
|
1.0
|
CA
|
C:CYS238
|
3.7
|
30.7
|
1.0
|
NE2
|
C:HIS179
|
3.9
|
41.8
|
1.0
|
CD2
|
C:HIS179
|
4.1
|
41.9
|
1.0
|
N
|
C:CYS176
|
4.1
|
40.1
|
1.0
|
N
|
C:ASN239
|
4.3
|
31.0
|
1.0
|
CA
|
C:CYS176
|
4.4
|
37.5
|
1.0
|
O
|
C:MET237
|
4.4
|
29.7
|
1.0
|
C
|
C:CYS238
|
4.5
|
34.7
|
1.0
|
CA
|
C:CYS242
|
4.6
|
38.2
|
1.0
|
N
|
C:HIS179
|
4.7
|
44.6
|
1.0
|
CA
|
C:HIS179
|
4.8
|
39.1
|
1.0
|
CE
|
D:MET243
|
4.8
|
35.2
|
1.0
|
N
|
C:CYS238
|
4.9
|
32.8
|
1.0
|
O
|
C:ASN239
|
4.9
|
34.3
|
1.0
|
CG
|
C:ARG175
|
4.9
|
38.5
|
1.0
|
O
|
C:CYS176
|
5.0
|
40.5
|
1.0
|
|
Zinc binding site 4 out
of 4 in 5lgy
Go back to
Zinc Binding Sites List in 5lgy
Zinc binding site 4 out
of 4 in the Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Lysine 120-Acetylated P53 Dna Binding Domain in A Complex with the Bax Response Element. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn301
b:37.0
occ:1.00
|
ND1
|
D:HIS179
|
2.2
|
40.9
|
1.0
|
SG
|
D:CYS176
|
2.3
|
47.7
|
1.0
|
SG
|
D:CYS238
|
2.4
|
37.2
|
1.0
|
SG
|
D:CYS242
|
2.4
|
37.0
|
1.0
|
CB
|
D:CYS242
|
3.0
|
32.9
|
1.0
|
CE1
|
D:HIS179
|
3.0
|
40.2
|
1.0
|
CG
|
D:HIS179
|
3.2
|
37.3
|
1.0
|
CB
|
D:CYS176
|
3.2
|
36.3
|
1.0
|
CB
|
D:CYS238
|
3.4
|
29.5
|
1.0
|
CB
|
D:HIS179
|
3.6
|
34.8
|
1.0
|
N
|
D:CYS176
|
3.9
|
38.7
|
1.0
|
CA
|
D:CYS238
|
3.9
|
31.6
|
1.0
|
CA
|
D:CYS176
|
4.1
|
32.5
|
1.0
|
NE2
|
D:HIS179
|
4.2
|
39.0
|
1.0
|
CD2
|
D:HIS179
|
4.2
|
33.4
|
1.0
|
CA
|
D:CYS242
|
4.4
|
37.6
|
1.0
|
N
|
D:ASN239
|
4.5
|
28.7
|
1.0
|
N
|
D:HIS179
|
4.6
|
34.1
|
1.0
|
O
|
D:MET237
|
4.7
|
35.2
|
1.0
|
C
|
D:CYS238
|
4.7
|
32.2
|
1.0
|
CA
|
D:HIS179
|
4.7
|
36.7
|
1.0
|
CE
|
C:MET243
|
4.8
|
41.1
|
1.0
|
O
|
D:CYS176
|
4.9
|
38.2
|
1.0
|
SD
|
C:MET243
|
4.9
|
49.1
|
1.0
|
C
|
D:CYS176
|
4.9
|
36.9
|
1.0
|
O
|
D:ASN239
|
4.9
|
34.8
|
1.0
|
|
Reference:
R.Vainer,
S.Cohen,
A.Shahar,
R.Zarivach,
E.Arbely.
Structural Basis For P53 LYS120-Acetylation-Dependent Dna-Binding Mode. J.Mol.Biol. V. 428 3013 2016.
ISSN: ESSN 1089-8638
PubMed: 27338200
DOI: 10.1016/J.JMB.2016.06.009
Page generated: Sun Oct 27 21:01:26 2024
|