Zinc in PDB 3hsv: Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2
Protein crystallography data
The structure of Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2, PDB code: 3hsv
was solved by
M.Zhuang,
B.A.Schulman,
D.Miller,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
31.23 /
1.43
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
88.953,
43.086,
87.453,
90.00,
118.15,
90.00
|
R / Rfree (%)
|
17.4 /
20.6
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2
(pdb code 3hsv). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the
Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2, PDB code: 3hsv:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
Zinc binding site 1 out
of 5 in 3hsv
Go back to
Zinc Binding Sites List in 3hsv
Zinc binding site 1 out
of 5 in the Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn2
b:11.1
occ:0.50
|
ZN
|
A:ZN2
|
0.0
|
11.1
|
0.5
|
ZN
|
A:ZN2
|
1.7
|
12.2
|
0.5
|
OE2
|
A:GLU113
|
2.0
|
7.3
|
1.0
|
OE2
|
A:GLU160
|
2.1
|
9.6
|
1.0
|
O
|
A:HOH407
|
2.1
|
8.5
|
0.5
|
CD
|
A:GLU160
|
2.7
|
10.1
|
1.0
|
OE1
|
A:GLU160
|
2.8
|
9.8
|
1.0
|
CD
|
A:GLU113
|
2.9
|
8.6
|
1.0
|
OE1
|
A:GLU113
|
3.1
|
11.1
|
1.0
|
CE2
|
A:PHE158
|
4.0
|
7.2
|
1.0
|
CG
|
A:GLU160
|
4.1
|
8.6
|
1.0
|
NZ
|
A:LYS103
|
4.1
|
17.6
|
1.0
|
CE
|
A:LYS103
|
4.3
|
14.5
|
1.0
|
CG
|
A:GLU113
|
4.3
|
8.1
|
1.0
|
CD2
|
A:PHE158
|
4.4
|
7.1
|
1.0
|
O
|
A:HOH185
|
4.5
|
8.3
|
1.0
|
O
|
A:HOH236
|
4.5
|
37.2
|
1.0
|
|
Zinc binding site 2 out
of 5 in 3hsv
Go back to
Zinc Binding Sites List in 3hsv
Zinc binding site 2 out
of 5 in the Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn2
b:12.2
occ:0.50
|
ZN
|
A:ZN2
|
0.0
|
12.2
|
0.5
|
ZN
|
A:ZN2
|
1.7
|
11.1
|
0.5
|
O
|
A:HOH407
|
2.1
|
8.5
|
0.5
|
OE2
|
A:GLU160
|
2.1
|
9.6
|
1.0
|
OE1
|
A:GLU113
|
2.1
|
11.1
|
1.0
|
OE2
|
A:GLU113
|
2.4
|
7.3
|
1.0
|
NZ
|
A:LYS103
|
2.6
|
17.6
|
1.0
|
CD
|
A:GLU113
|
2.6
|
8.6
|
1.0
|
CE
|
A:LYS103
|
2.7
|
14.5
|
1.0
|
CD
|
A:GLU160
|
3.1
|
10.1
|
1.0
|
OE1
|
A:GLU160
|
3.3
|
9.8
|
1.0
|
O
|
A:HOH185
|
3.7
|
8.3
|
1.0
|
CG
|
A:GLU113
|
4.1
|
8.1
|
1.0
|
CD
|
A:LYS103
|
4.2
|
10.4
|
1.0
|
CG
|
A:GLU160
|
4.4
|
8.6
|
1.0
|
O
|
A:HOH188
|
4.5
|
22.6
|
1.0
|
O
|
A:HOH236
|
4.5
|
37.2
|
1.0
|
O
|
A:HOH232
|
4.8
|
14.8
|
1.0
|
CB
|
A:GLU113
|
4.9
|
7.3
|
1.0
|
CE2
|
A:PHE158
|
4.9
|
7.2
|
1.0
|
CG
|
A:LYS103
|
4.9
|
7.0
|
1.0
|
CD2
|
A:PHE158
|
5.0
|
7.1
|
1.0
|
|
Zinc binding site 3 out
of 5 in 3hsv
Go back to
Zinc Binding Sites List in 3hsv
Zinc binding site 3 out
of 5 in the Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn3
b:8.7
occ:0.50
|
ZN
|
B:ZN3
|
0.0
|
8.7
|
0.5
|
ZN
|
B:ZN3
|
1.8
|
11.7
|
0.5
|
OE2
|
B:GLU113
|
1.9
|
8.0
|
1.0
|
OE2
|
B:GLU160
|
2.2
|
7.5
|
1.0
|
O
|
B:HOH408
|
2.2
|
3.5
|
0.5
|
CD
|
B:GLU113
|
2.8
|
8.0
|
1.0
|
CD
|
B:GLU160
|
2.9
|
6.9
|
1.0
|
OE1
|
B:GLU113
|
2.9
|
10.9
|
1.0
|
OE1
|
B:GLU160
|
3.1
|
6.7
|
1.0
|
NZ
|
B:LYS103
|
3.8
|
16.0
|
0.5
|
NZ
|
B:LYS103
|
3.9
|
16.3
|
0.5
|
CE2
|
B:PHE158
|
3.9
|
5.9
|
1.0
|
CG
|
B:GLU113
|
4.2
|
7.5
|
1.0
|
CG
|
B:GLU160
|
4.2
|
5.8
|
1.0
|
CD2
|
B:PHE158
|
4.3
|
5.3
|
1.0
|
CE
|
B:LYS103
|
4.4
|
14.4
|
0.5
|
CE
|
B:LYS103
|
4.5
|
14.1
|
0.5
|
O
|
B:HOH191
|
4.5
|
7.5
|
1.0
|
O
|
B:HOH387
|
4.9
|
31.2
|
1.0
|
|
Zinc binding site 4 out
of 5 in 3hsv
Go back to
Zinc Binding Sites List in 3hsv
Zinc binding site 4 out
of 5 in the Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn3
b:11.7
occ:0.50
|
ZN
|
B:ZN3
|
0.0
|
11.7
|
0.5
|
ZN
|
B:ZN3
|
1.8
|
8.7
|
0.5
|
NZ
|
B:LYS103
|
2.0
|
16.0
|
0.5
|
OE2
|
B:GLU160
|
2.1
|
7.5
|
1.0
|
O
|
B:HOH408
|
2.1
|
3.5
|
0.5
|
OE1
|
B:GLU113
|
2.1
|
10.9
|
1.0
|
NZ
|
B:LYS103
|
2.3
|
16.3
|
0.5
|
OE2
|
B:GLU113
|
2.6
|
8.0
|
1.0
|
CD
|
B:GLU113
|
2.6
|
8.0
|
1.0
|
CE
|
B:LYS103
|
2.8
|
14.4
|
0.5
|
CE
|
B:LYS103
|
2.8
|
14.1
|
0.5
|
CD
|
B:GLU160
|
3.0
|
6.9
|
1.0
|
OE1
|
B:GLU160
|
3.4
|
6.7
|
1.0
|
O
|
B:HOH191
|
3.6
|
7.5
|
1.0
|
CG
|
B:GLU113
|
4.1
|
7.5
|
1.0
|
CD
|
B:LYS103
|
4.2
|
11.8
|
0.5
|
CD
|
B:LYS103
|
4.2
|
11.8
|
0.5
|
O
|
B:HOH262
|
4.3
|
27.0
|
1.0
|
CG
|
B:GLU160
|
4.3
|
5.8
|
1.0
|
CB
|
B:GLU113
|
4.8
|
6.5
|
1.0
|
CG
|
B:LYS103
|
4.8
|
8.2
|
0.5
|
CD2
|
B:PHE158
|
4.8
|
5.3
|
1.0
|
CE2
|
B:PHE158
|
4.8
|
5.9
|
1.0
|
OG
|
B:SER105
|
4.9
|
6.3
|
1.0
|
O
|
B:HOH387
|
4.9
|
31.2
|
1.0
|
|
Zinc binding site 5 out
of 5 in 3hsv
Go back to
Zinc Binding Sites List in 3hsv
Zinc binding site 5 out
of 5 in the Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases: Spopmathx-MACROH2ASBCPEP2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
M:Zn1
b:22.0
occ:1.00
|
O
|
M:HOH308
|
2.0
|
16.0
|
0.5
|
SG
|
A:CYS93
|
2.0
|
10.8
|
1.0
|
O
|
M:HOH308
|
2.1
|
16.0
|
0.5
|
OD2
|
M:ASP180
|
2.3
|
3.0
|
1.0
|
CG
|
M:ASP180
|
2.9
|
2.8
|
1.0
|
CB
|
M:ASP180
|
3.0
|
2.4
|
1.0
|
CB
|
A:CYS93
|
3.3
|
7.2
|
1.0
|
N
|
M:GLY181
|
3.4
|
2.6
|
1.0
|
CE
|
B:LYS134
|
3.5
|
6.4
|
1.0
|
C
|
M:ASP180
|
3.8
|
2.2
|
1.0
|
CD2
|
B:LEU76
|
3.9
|
10.8
|
1.0
|
OE1
|
A:GLN127
|
3.9
|
7.1
|
1.0
|
CA
|
M:ASP180
|
3.9
|
2.1
|
1.0
|
CA
|
M:GLY181
|
4.0
|
5.1
|
1.0
|
O
|
A:HOH177
|
4.0
|
3.7
|
0.5
|
NZ
|
B:LYS134
|
4.0
|
5.6
|
1.0
|
OD1
|
M:ASP180
|
4.0
|
3.8
|
1.0
|
OH
|
B:TYR87
|
4.1
|
7.1
|
1.0
|
C
|
M:GLY181
|
4.3
|
7.1
|
1.0
|
CA
|
A:CYS93
|
4.5
|
6.7
|
1.0
|
O
|
M:ASP180
|
4.6
|
2.0
|
1.0
|
O
|
M:GLY181
|
4.8
|
8.9
|
1.0
|
CD
|
B:LYS134
|
4.9
|
5.7
|
1.0
|
CE1
|
B:TYR87
|
4.9
|
4.6
|
1.0
|
CZ
|
B:TYR87
|
5.0
|
5.2
|
1.0
|
|
Reference:
M.Zhuang,
M.F.Calabrese,
J.Liu,
M.B.Waddell,
A.Nourse,
M.Hammel,
D.J.Miller,
H.Walden,
D.M.Duda,
S.N.Seyedin,
T.Hoggard,
J.W.Harper,
K.P.White,
B.A.Schulman.
Structures of Spop-Substrate Complexes: Insights Into Molecular Architectures of Btb-CUL3 Ubiquitin Ligases. Mol.Cell V. 36 39 2009.
ISSN: ISSN 1097-2765
PubMed: 19818708
DOI: 10.1016/J.MOLCEL.2009.09.022
Page generated: Sat Oct 26 06:42:32 2024
|