Zinc in PDB 6mii: Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex
Enzymatic activity of Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex
All present enzymatic activity of Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex:
3.6.4.12;
Protein crystallography data
The structure of Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex, PDB code: 6mii
was solved by
E.J.Enemark,
M.Meagher,
L.B.Epling,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
44.70 /
3.15
|
Space group
|
P 41 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
186.665,
186.665,
281.489,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.8 /
24.1
|
Other elements in 6mii:
The structure of Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex
(pdb code 6mii). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex, PDB code: 6mii:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 6mii
Go back to
Zinc Binding Sites List in 6mii
Zinc binding site 1 out
of 6 in the Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn2002
b:0.5
occ:1.00
|
SG
|
A:CYS174
|
2.1
|
0.4
|
1.0
|
SG
|
A:CYS149
|
2.1
|
0.8
|
1.0
|
SG
|
A:CYS171
|
2.1
|
0.4
|
1.0
|
ND1
|
A:HIS144
|
2.1
|
0.3
|
1.0
|
CB
|
A:CYS149
|
2.8
|
0.8
|
1.0
|
CB
|
A:CYS171
|
2.9
|
0.1
|
1.0
|
CE1
|
A:HIS144
|
3.1
|
0.3
|
1.0
|
CG
|
A:HIS144
|
3.1
|
0.8
|
1.0
|
CB
|
A:HIS144
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS174
|
3.5
|
0.6
|
1.0
|
NE2
|
A:HIS144
|
4.2
|
0.2
|
1.0
|
CD2
|
A:HIS144
|
4.2
|
0.9
|
1.0
|
N
|
A:CYS174
|
4.2
|
0.8
|
1.0
|
CA
|
A:CYS149
|
4.3
|
0.3
|
1.0
|
CA
|
A:CYS171
|
4.3
|
1.0
|
1.0
|
O
|
A:LYS176
|
4.3
|
0.2
|
1.0
|
CA
|
A:CYS174
|
4.5
|
0.0
|
1.0
|
C
|
A:CYS171
|
4.8
|
0.5
|
1.0
|
N
|
A:LYS176
|
4.9
|
0.0
|
1.0
|
C
|
A:LYS173
|
4.9
|
0.4
|
1.0
|
CA
|
A:HIS144
|
4.9
|
0.8
|
1.0
|
O
|
A:CYS171
|
4.9
|
0.0
|
1.0
|
N
|
A:GLY175
|
4.9
|
0.6
|
1.0
|
CB
|
A:LYS176
|
5.0
|
0.5
|
1.0
|
|
Zinc binding site 2 out
of 6 in 6mii
Go back to
Zinc Binding Sites List in 6mii
Zinc binding site 2 out
of 6 in the Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn2002
b:0.1
occ:1.00
|
SG
|
B:CYS174
|
2.1
|
0.0
|
1.0
|
SG
|
B:CYS171
|
2.1
|
0.7
|
1.0
|
SG
|
B:CYS149
|
2.1
|
0.7
|
1.0
|
ND1
|
B:HIS144
|
2.1
|
0.9
|
1.0
|
CB
|
B:CYS149
|
2.9
|
0.6
|
1.0
|
CB
|
B:CYS171
|
3.0
|
0.9
|
1.0
|
CE1
|
B:HIS144
|
3.0
|
0.1
|
1.0
|
CG
|
B:HIS144
|
3.1
|
0.5
|
1.0
|
CB
|
B:HIS144
|
3.5
|
0.5
|
1.0
|
CB
|
B:CYS174
|
3.6
|
1.0
|
1.0
|
N
|
B:CYS174
|
4.1
|
0.5
|
1.0
|
NE2
|
B:HIS144
|
4.2
|
0.5
|
1.0
|
CD2
|
B:HIS144
|
4.2
|
0.2
|
1.0
|
CA
|
B:CYS149
|
4.3
|
1.0
|
1.0
|
CA
|
B:CYS171
|
4.4
|
0.1
|
1.0
|
CA
|
B:CYS174
|
4.4
|
0.5
|
1.0
|
O
|
B:LYS176
|
4.4
|
0.8
|
1.0
|
C
|
B:LYS173
|
4.7
|
0.7
|
1.0
|
CB
|
B:LYS173
|
4.7
|
0.3
|
1.0
|
N
|
B:GLY175
|
4.9
|
0.1
|
1.0
|
CA
|
B:HIS144
|
5.0
|
0.1
|
1.0
|
|
Zinc binding site 3 out
of 6 in 6mii
Go back to
Zinc Binding Sites List in 6mii
Zinc binding site 3 out
of 6 in the Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn2002
b:0.6
occ:1.00
|
SG
|
C:CYS174
|
2.1
|
1.0
|
1.0
|
SG
|
C:CYS149
|
2.1
|
0.9
|
1.0
|
ND1
|
C:HIS144
|
2.1
|
0.4
|
1.0
|
SG
|
C:CYS171
|
2.1
|
0.8
|
1.0
|
CB
|
C:CYS171
|
2.9
|
0.9
|
1.0
|
CG
|
C:HIS144
|
3.0
|
0.6
|
1.0
|
CB
|
C:CYS149
|
3.1
|
0.4
|
1.0
|
CE1
|
C:HIS144
|
3.1
|
0.9
|
1.0
|
CB
|
C:HIS144
|
3.3
|
1.0
|
1.0
|
CB
|
C:CYS174
|
3.4
|
0.2
|
1.0
|
N
|
C:CYS174
|
4.2
|
0.9
|
1.0
|
CD2
|
C:HIS144
|
4.2
|
0.8
|
1.0
|
O
|
C:LYS176
|
4.2
|
0.0
|
1.0
|
NE2
|
C:HIS144
|
4.2
|
0.4
|
1.0
|
CA
|
C:CYS174
|
4.4
|
1.0
|
1.0
|
CA
|
C:CYS171
|
4.4
|
0.2
|
1.0
|
CA
|
C:CYS149
|
4.5
|
0.1
|
1.0
|
CA
|
C:HIS144
|
4.8
|
0.6
|
1.0
|
N
|
C:GLY175
|
4.9
|
0.8
|
1.0
|
C
|
C:LYS173
|
4.9
|
0.2
|
1.0
|
N
|
C:LYS176
|
4.9
|
0.6
|
1.0
|
C
|
C:CYS171
|
4.9
|
0.6
|
1.0
|
|
Zinc binding site 4 out
of 6 in 6mii
Go back to
Zinc Binding Sites List in 6mii
Zinc binding site 4 out
of 6 in the Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn2002
b:0.3
occ:1.00
|
ND1
|
D:HIS144
|
2.1
|
0.0
|
1.0
|
SG
|
D:CYS171
|
2.1
|
0.4
|
1.0
|
SG
|
D:CYS149
|
2.1
|
0.5
|
1.0
|
SG
|
D:CYS174
|
2.1
|
0.4
|
1.0
|
CB
|
D:CYS149
|
2.7
|
1.0
|
1.0
|
CE1
|
D:HIS144
|
2.9
|
0.5
|
1.0
|
CG
|
D:HIS144
|
3.2
|
0.2
|
1.0
|
CB
|
D:CYS171
|
3.2
|
0.1
|
1.0
|
CB
|
D:CYS174
|
3.5
|
0.0
|
1.0
|
CB
|
D:HIS144
|
3.6
|
0.8
|
1.0
|
N
|
D:CYS174
|
4.0
|
0.7
|
1.0
|
NE2
|
D:HIS144
|
4.1
|
0.9
|
1.0
|
CA
|
D:CYS149
|
4.1
|
0.6
|
1.0
|
CD2
|
D:HIS144
|
4.2
|
0.5
|
1.0
|
CA
|
D:CYS174
|
4.3
|
0.1
|
1.0
|
CB
|
D:LYS173
|
4.5
|
0.0
|
1.0
|
O
|
D:LYS176
|
4.5
|
0.4
|
1.0
|
C
|
D:LYS173
|
4.6
|
0.6
|
1.0
|
CA
|
D:CYS171
|
4.6
|
0.0
|
1.0
|
N
|
D:GLY175
|
4.9
|
0.6
|
1.0
|
N
|
D:LYS173
|
4.9
|
0.9
|
1.0
|
CA
|
D:LYS173
|
4.9
|
1.0
|
1.0
|
N
|
D:CYS149
|
4.9
|
0.5
|
1.0
|
|
Zinc binding site 5 out
of 6 in 6mii
Go back to
Zinc Binding Sites List in 6mii
Zinc binding site 5 out
of 6 in the Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn2002
b:0.4
occ:1.00
|
ND1
|
E:HIS144
|
2.1
|
0.3
|
1.0
|
SG
|
E:CYS149
|
2.1
|
0.7
|
1.0
|
SG
|
E:CYS171
|
2.1
|
0.0
|
1.0
|
SG
|
E:CYS174
|
2.1
|
0.2
|
1.0
|
CB
|
E:CYS149
|
2.7
|
0.0
|
1.0
|
CB
|
E:CYS171
|
2.9
|
0.7
|
1.0
|
CE1
|
E:HIS144
|
3.0
|
1.0
|
1.0
|
CG
|
E:HIS144
|
3.1
|
0.8
|
1.0
|
CB
|
E:HIS144
|
3.4
|
0.6
|
1.0
|
CB
|
E:CYS174
|
3.6
|
0.0
|
1.0
|
CA
|
E:CYS149
|
4.1
|
0.2
|
1.0
|
N
|
E:CYS174
|
4.1
|
0.4
|
1.0
|
NE2
|
E:HIS144
|
4.1
|
0.6
|
1.0
|
CD2
|
E:HIS144
|
4.2
|
0.5
|
1.0
|
CA
|
E:CYS171
|
4.3
|
0.7
|
1.0
|
CA
|
E:CYS174
|
4.5
|
0.1
|
1.0
|
CB
|
E:LYS173
|
4.6
|
0.8
|
1.0
|
C
|
E:LYS173
|
4.7
|
0.6
|
1.0
|
C
|
E:CYS171
|
4.8
|
0.4
|
1.0
|
O
|
E:LYS176
|
4.8
|
0.6
|
1.0
|
N
|
E:CYS149
|
4.9
|
0.7
|
1.0
|
O
|
E:CYS171
|
4.9
|
0.9
|
1.0
|
CA
|
E:HIS144
|
4.9
|
0.5
|
1.0
|
N
|
E:LYS173
|
5.0
|
0.2
|
1.0
|
C
|
E:CYS149
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 6 out
of 6 in 6mii
Go back to
Zinc Binding Sites List in 6mii
Zinc binding site 6 out
of 6 in the Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Crystal Structure of Minichromosome Maintenance Protein Mcm/Dna Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Zn2002
b:0.3
occ:1.00
|
SG
|
F:CYS149
|
2.1
|
0.1
|
1.0
|
ND1
|
F:HIS144
|
2.1
|
0.3
|
1.0
|
SG
|
F:CYS171
|
2.1
|
0.7
|
1.0
|
SG
|
F:CYS174
|
2.1
|
0.8
|
1.0
|
CB
|
F:CYS171
|
2.9
|
0.9
|
1.0
|
CB
|
F:CYS149
|
3.0
|
0.7
|
1.0
|
CG
|
F:HIS144
|
3.1
|
0.1
|
1.0
|
CE1
|
F:HIS144
|
3.1
|
0.8
|
1.0
|
CB
|
F:HIS144
|
3.4
|
0.9
|
1.0
|
CB
|
F:CYS174
|
3.5
|
0.4
|
1.0
|
N
|
F:CYS174
|
4.1
|
0.0
|
1.0
|
NE2
|
F:HIS144
|
4.2
|
0.8
|
1.0
|
CD2
|
F:HIS144
|
4.2
|
0.3
|
1.0
|
O
|
F:LYS176
|
4.2
|
0.7
|
1.0
|
CA
|
F:CYS149
|
4.4
|
0.4
|
1.0
|
CA
|
F:CYS171
|
4.4
|
0.3
|
1.0
|
CA
|
F:CYS174
|
4.4
|
0.2
|
1.0
|
C
|
F:LYS173
|
4.8
|
0.8
|
1.0
|
CA
|
F:HIS144
|
4.9
|
0.7
|
1.0
|
CB
|
F:LYS173
|
4.9
|
0.7
|
1.0
|
C
|
F:CYS171
|
4.9
|
0.2
|
1.0
|
N
|
F:GLY175
|
4.9
|
0.9
|
1.0
|
|
Reference:
M.Meagher,
L.B.Epling,
E.J.Enemark.
Dna Translocation Mechanism of the Mcm Complex and Implications For Replication Initiation. Nat Commun V. 10 3117 2019.
ISSN: ESSN 2041-1723
PubMed: 31308367
DOI: 10.1038/S41467-019-11074-3
Page generated: Tue Oct 29 03:12:30 2024
|