Zinc in PDB 5z58: Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom.
Enzymatic activity of Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom.
All present enzymatic activity of Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom.:
3.6.4.13;
5.2.1.8;
Other elements in 5z58:
The structure of Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom. also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom.
(pdb code 5z58). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom., PDB code: 5z58:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 5z58
Go back to
Zinc Binding Sites List in 5z58
Zinc binding site 1 out
of 4 in the Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom.
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
6:Zn201
b:0.0
occ:1.00
|
SG
|
6:CYS23
|
2.4
|
0.1
|
1.0
|
SG
|
6:CYS26
|
2.5
|
0.4
|
1.0
|
SG
|
6:CYS58
|
2.5
|
0.7
|
1.0
|
SG
|
6:CYS61
|
2.7
|
0.5
|
1.0
|
NZ
|
6:LYS25
|
2.7
|
0.9
|
1.0
|
CE
|
6:LYS25
|
3.2
|
0.5
|
1.0
|
CB
|
6:CYS26
|
3.4
|
0.7
|
1.0
|
CB
|
6:CYS61
|
3.4
|
0.5
|
1.0
|
N
|
6:CYS61
|
3.6
|
0.5
|
1.0
|
N
|
6:CYS26
|
3.6
|
0.1
|
1.0
|
CB
|
6:CYS58
|
3.8
|
0.2
|
1.0
|
CB
|
6:CYS23
|
3.9
|
0.9
|
1.0
|
CB
|
6:LYS25
|
4.0
|
0.4
|
1.0
|
CA
|
6:CYS26
|
4.1
|
0.4
|
1.0
|
CB
|
6:ILE60
|
4.1
|
0.3
|
1.0
|
CA
|
6:CYS61
|
4.1
|
0.4
|
1.0
|
CD
|
6:LYS25
|
4.4
|
0.7
|
1.0
|
CG
|
6:LYS25
|
4.4
|
0.9
|
1.0
|
N
|
6:CYS23
|
4.6
|
0.3
|
1.0
|
C
|
6:LYS25
|
4.6
|
1.0
|
1.0
|
C
|
6:ILE60
|
4.7
|
0.4
|
1.0
|
CA
|
6:LYS25
|
4.7
|
1.0
|
1.0
|
CG2
|
6:ILE60
|
4.8
|
0.2
|
1.0
|
CA
|
6:ILE60
|
4.8
|
0.1
|
1.0
|
CA
|
6:CYS23
|
4.8
|
0.2
|
1.0
|
N
|
6:ILE60
|
4.9
|
0.4
|
1.0
|
N
|
6:LYS25
|
4.9
|
0.2
|
1.0
|
CG1
|
6:ILE60
|
4.9
|
0.4
|
1.0
|
|
Zinc binding site 2 out
of 4 in 5z58
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Zinc Binding Sites List in 5z58
Zinc binding site 2 out
of 4 in the Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom.
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
6:Zn202
b:0.3
occ:1.00
|
SG
|
6:CYS49
|
2.3
|
0.3
|
1.0
|
SG
|
6:CYS46
|
2.5
|
0.1
|
1.0
|
CD
|
6:LYS13
|
2.5
|
0.5
|
1.0
|
CB
|
6:LYS13
|
2.5
|
0.8
|
1.0
|
CG
|
6:LYS13
|
2.8
|
0.9
|
1.0
|
SG
|
6:CYS85
|
3.1
|
0.7
|
1.0
|
SG
|
6:CYS11
|
3.4
|
0.9
|
1.0
|
CB
|
6:CYS49
|
3.6
|
0.8
|
1.0
|
N
|
6:CYS49
|
3.7
|
0.4
|
1.0
|
CA
|
6:LYS13
|
3.7
|
0.9
|
1.0
|
CE
|
6:LYS13
|
3.8
|
0.9
|
1.0
|
N
|
6:LYS13
|
3.9
|
0.3
|
1.0
|
CB
|
6:GLU48
|
4.1
|
0.8
|
1.0
|
CA
|
6:CYS49
|
4.1
|
0.7
|
1.0
|
CB
|
6:CYS11
|
4.2
|
0.1
|
1.0
|
CB
|
6:CYS46
|
4.2
|
0.8
|
1.0
|
C
|
6:GLU48
|
4.3
|
0.4
|
1.0
|
NZ
|
6:LYS13
|
4.4
|
0.0
|
1.0
|
C
|
6:LYS13
|
4.5
|
0.3
|
1.0
|
CA
|
6:GLU48
|
4.7
|
0.5
|
1.0
|
CB
|
6:CYS85
|
4.8
|
0.6
|
1.0
|
O
|
6:LYS13
|
4.8
|
0.3
|
1.0
|
O
|
6:GLU48
|
4.9
|
96.0
|
1.0
|
|
Zinc binding site 3 out
of 4 in 5z58
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Zinc Binding Sites List in 5z58
Zinc binding site 3 out
of 4 in the Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom.
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
6:Zn203
b:0.7
occ:1.00
|
SG
|
6:CYS33
|
2.3
|
0.3
|
1.0
|
SG
|
6:CYS75
|
2.4
|
0.6
|
1.0
|
SG
|
6:CYS30
|
2.5
|
0.9
|
1.0
|
SG
|
6:CYS72
|
2.5
|
0.4
|
1.0
|
CB
|
6:CYS33
|
2.7
|
0.5
|
1.0
|
N
|
6:CYS33
|
3.0
|
0.4
|
1.0
|
CA
|
6:CYS33
|
3.4
|
0.2
|
1.0
|
CB
|
6:CYS75
|
3.4
|
1.0
|
1.0
|
CB
|
6:CYS30
|
3.7
|
0.1
|
1.0
|
CB
|
6:CYS72
|
3.7
|
0.8
|
1.0
|
N
|
6:CYS72
|
4.1
|
0.3
|
1.0
|
C
|
6:ILE32
|
4.1
|
0.3
|
1.0
|
N
|
6:CYS75
|
4.3
|
0.7
|
1.0
|
N
|
6:ILE32
|
4.3
|
0.1
|
1.0
|
C
|
6:CYS33
|
4.5
|
0.4
|
1.0
|
CA
|
6:CYS75
|
4.5
|
0.2
|
1.0
|
CA
|
6:CYS72
|
4.5
|
0.1
|
1.0
|
CA
|
6:ILE32
|
4.5
|
0.3
|
1.0
|
CB
|
6:ILE32
|
4.5
|
0.8
|
1.0
|
C
|
6:CYS30
|
4.6
|
0.2
|
1.0
|
CA
|
6:CYS30
|
4.8
|
0.2
|
1.0
|
O
|
6:CYS30
|
4.8
|
0.8
|
1.0
|
N
|
6:ASP34
|
4.8
|
0.7
|
1.0
|
N
|
6:VAL31
|
4.9
|
0.2
|
1.0
|
|
Zinc binding site 4 out
of 4 in 5z58
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Zinc Binding Sites List in 5z58
Zinc binding site 4 out
of 4 in the Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom.
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Cryo-Em Structure of A Human Activated Spliceosome (Early Bact) at 4.9 Angstrom. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
M:Zn500
b:60.1
occ:1.00
|
SG
|
M:CYS217
|
2.2
|
0.9
|
1.0
|
SG
|
M:CYS202
|
2.2
|
31.2
|
1.0
|
SG
|
M:CYS211
|
2.5
|
94.9
|
1.0
|
CB
|
M:CYS202
|
3.0
|
61.4
|
1.0
|
NE2
|
M:HIS221
|
3.0
|
0.5
|
1.0
|
CD2
|
M:HIS221
|
3.2
|
1.0
|
1.0
|
CB
|
M:CYS217
|
3.3
|
0.6
|
1.0
|
CB
|
M:CYS211
|
3.4
|
0.6
|
1.0
|
N2
|
G:G1
|
3.4
|
99.5
|
1.0
|
N1
|
G:G1
|
3.8
|
0.2
|
1.0
|
C2
|
G:G1
|
4.1
|
0.1
|
1.0
|
CE1
|
M:HIS221
|
4.2
|
86.1
|
1.0
|
CB
|
M:TYR205
|
4.4
|
0.5
|
1.0
|
CA
|
M:CYS202
|
4.4
|
86.2
|
1.0
|
CG
|
M:HIS221
|
4.4
|
0.0
|
1.0
|
CA
|
M:CYS211
|
4.5
|
0.3
|
1.0
|
CA
|
M:CYS217
|
4.7
|
0.3
|
1.0
|
CB
|
M:PHE219
|
4.7
|
0.0
|
1.0
|
ND1
|
M:HIS221
|
4.9
|
86.4
|
1.0
|
N
|
M:TYR205
|
4.9
|
0.8
|
1.0
|
C6
|
G:G1
|
5.0
|
0.3
|
1.0
|
|
Reference:
X.Zhang,
C.Yan,
X.Zhan,
L.Li,
J.Lei,
Y.Shi.
Structure of the Human Activated Spliceosome in Three Conformational States. Cell Res. V. 28 307 2018.
ISSN: ISSN 1748-7838
PubMed: 29360106
DOI: 10.1038/CR.2018.14
Page generated: Mon Oct 28 16:33:26 2024
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