Zinc in PDB 5of9: Crystal Structure of Human MORC2 (Residues 1-603)
Protein crystallography data
The structure of Crystal Structure of Human MORC2 (Residues 1-603), PDB code: 5of9
was solved by
C.H.Douse,
M.Shamin,
Y.Modis,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
64.91 /
1.81
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
66.170,
127.930,
80.190,
90.00,
101.22,
90.00
|
R / Rfree (%)
|
16.1 /
18.8
|
Other elements in 5of9:
The structure of Crystal Structure of Human MORC2 (Residues 1-603) also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Human MORC2 (Residues 1-603)
(pdb code 5of9). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Crystal Structure of Human MORC2 (Residues 1-603), PDB code: 5of9:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 5of9
Go back to
Zinc Binding Sites List in 5of9
Zinc binding site 1 out
of 2 in the Crystal Structure of Human MORC2 (Residues 1-603)
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 Human MORC2 (Residues 1-603) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn701
b:35.8
occ:1.00
|
SG
|
A:CYS536
|
2.3
|
37.8
|
1.0
|
SG
|
A:CYS525
|
2.3
|
35.0
|
1.0
|
SG
|
A:CYS502
|
2.3
|
35.6
|
1.0
|
SG
|
A:CYS499
|
2.4
|
34.9
|
1.0
|
HA
|
A:CYS536
|
2.8
|
48.1
|
1.0
|
HB3
|
A:CYS502
|
3.0
|
42.9
|
1.0
|
HB2
|
A:CYS525
|
3.0
|
43.0
|
1.0
|
HB3
|
A:CYS499
|
3.0
|
35.2
|
1.0
|
H
|
A:CYS525
|
3.0
|
45.7
|
1.0
|
HB2
|
A:CYS499
|
3.0
|
35.2
|
1.0
|
CB
|
A:CYS499
|
3.0
|
29.4
|
1.0
|
CB
|
A:CYS536
|
3.1
|
55.1
|
1.0
|
HB3
|
A:CYS536
|
3.1
|
66.2
|
1.0
|
H
|
A:CYS502
|
3.2
|
46.8
|
1.0
|
CB
|
A:CYS502
|
3.3
|
35.7
|
1.0
|
CB
|
A:CYS525
|
3.3
|
35.8
|
1.0
|
CA
|
A:CYS536
|
3.4
|
40.0
|
1.0
|
HB2
|
A:LEU501
|
3.8
|
41.6
|
1.0
|
N
|
A:CYS525
|
3.8
|
38.1
|
1.0
|
N
|
A:CYS502
|
3.8
|
39.0
|
1.0
|
HB2
|
A:CYS536
|
4.0
|
66.2
|
1.0
|
HB3
|
A:CYS525
|
4.0
|
43.0
|
1.0
|
HB2
|
A:CYS502
|
4.0
|
42.9
|
1.0
|
CA
|
A:CYS502
|
4.1
|
34.6
|
1.0
|
CA
|
A:CYS525
|
4.2
|
45.6
|
1.0
|
N
|
A:CYS536
|
4.2
|
42.6
|
1.0
|
HH21
|
A:ARG506
|
4.2
|
49.6
|
1.0
|
HB2
|
A:LYS504
|
4.3
|
40.6
|
1.0
|
H
|
A:CYS536
|
4.4
|
51.1
|
1.0
|
H
|
A:LEU501
|
4.4
|
42.3
|
1.0
|
H
|
A:LYS504
|
4.5
|
37.2
|
1.0
|
CA
|
A:CYS499
|
4.5
|
36.5
|
1.0
|
HA
|
A:CYS525
|
4.6
|
54.8
|
1.0
|
HE
|
A:ARG506
|
4.6
|
41.8
|
1.0
|
HA
|
A:VAL524
|
4.6
|
48.9
|
1.0
|
HB
|
A:VAL524
|
4.6
|
45.4
|
1.0
|
O
|
A:HOH1058
|
4.6
|
36.9
|
1.0
|
C
|
A:CYS536
|
4.6
|
36.5
|
1.0
|
H
|
A:LEU503
|
4.7
|
36.8
|
1.0
|
CB
|
A:LEU501
|
4.7
|
34.7
|
1.0
|
O
|
A:CYS536
|
4.7
|
34.9
|
1.0
|
HD2
|
A:LYS504
|
4.8
|
45.9
|
1.0
|
C
|
A:CYS502
|
4.8
|
30.6
|
1.0
|
HA
|
A:CYS499
|
4.9
|
43.9
|
1.0
|
C
|
A:LEU501
|
4.9
|
37.6
|
1.0
|
HA
|
A:CYS502
|
4.9
|
41.6
|
1.0
|
HD12
|
A:LEU501
|
4.9
|
58.6
|
1.0
|
C
|
A:VAL524
|
5.0
|
40.9
|
1.0
|
HB3
|
A:LEU501
|
5.0
|
41.6
|
1.0
|
N
|
A:LEU503
|
5.0
|
30.6
|
1.0
|
|
Zinc binding site 2 out
of 2 in 5of9
Go back to
Zinc Binding Sites List in 5of9
Zinc binding site 2 out
of 2 in the Crystal Structure of Human MORC2 (Residues 1-603)
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 Human MORC2 (Residues 1-603) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn701
b:50.5
occ:1.00
|
SG
|
B:CYS502
|
2.3
|
64.2
|
1.0
|
SG
|
B:CYS525
|
2.3
|
61.5
|
1.0
|
SG
|
B:CYS499
|
2.4
|
57.7
|
1.0
|
SG
|
B:CYS536
|
2.4
|
65.1
|
1.0
|
HB3
|
B:CYS499
|
2.8
|
66.2
|
1.0
|
HA
|
B:CYS536
|
2.8
|
80.3
|
1.0
|
CB
|
B:CYS499
|
2.9
|
55.3
|
1.0
|
HB2
|
B:CYS499
|
2.9
|
66.2
|
1.0
|
H
|
B:CYS502
|
3.0
|
67.1
|
1.0
|
HB3
|
B:CYS536
|
3.1
|
79.2
|
1.0
|
CB
|
B:CYS536
|
3.2
|
66.1
|
1.0
|
HB2
|
B:CYS525
|
3.2
|
77.6
|
1.0
|
H
|
B:CYS525
|
3.2
|
75.0
|
1.0
|
CB
|
B:CYS525
|
3.4
|
64.8
|
1.0
|
HB3
|
B:CYS502
|
3.5
|
81.3
|
1.0
|
CA
|
B:CYS536
|
3.5
|
67.0
|
1.0
|
CB
|
B:CYS502
|
3.5
|
67.8
|
1.0
|
HB2
|
B:LEU501
|
3.6
|
71.4
|
1.0
|
N
|
B:CYS502
|
3.7
|
56.0
|
1.0
|
N
|
B:CYS525
|
3.9
|
62.6
|
1.0
|
HB2
|
B:CYS536
|
4.1
|
79.2
|
1.0
|
HB3
|
B:CYS525
|
4.1
|
77.6
|
1.0
|
CA
|
B:CYS502
|
4.2
|
56.0
|
1.0
|
HH21
|
B:ARG506
|
4.3
|
0.1
|
1.0
|
CA
|
B:CYS525
|
4.3
|
64.2
|
1.0
|
HB2
|
B:CYS502
|
4.3
|
81.3
|
1.0
|
H
|
B:LEU501
|
4.3
|
65.8
|
1.0
|
N
|
B:CYS536
|
4.3
|
70.2
|
1.0
|
CA
|
B:CYS499
|
4.4
|
53.1
|
1.0
|
HB2
|
B:LYS504
|
4.4
|
65.1
|
1.0
|
CB
|
B:LEU501
|
4.5
|
59.6
|
1.0
|
H
|
B:LYS504
|
4.5
|
61.5
|
1.0
|
O
|
B:CYS536
|
4.6
|
78.9
|
1.0
|
HB
|
B:VAL524
|
4.6
|
74.2
|
1.0
|
C
|
B:CYS536
|
4.6
|
67.7
|
1.0
|
H
|
B:CYS536
|
4.6
|
84.0
|
1.0
|
HA
|
B:CYS525
|
4.7
|
76.9
|
1.0
|
HE
|
B:ARG506
|
4.7
|
92.6
|
1.0
|
HB3
|
B:LEU501
|
4.7
|
71.4
|
1.0
|
HA
|
B:VAL524
|
4.7
|
72.1
|
1.0
|
HA
|
B:CYS499
|
4.7
|
63.5
|
1.0
|
HD12
|
B:LEU501
|
4.8
|
77.1
|
1.0
|
C
|
B:LEU501
|
4.8
|
61.2
|
1.0
|
H
|
B:LEU503
|
4.8
|
61.8
|
1.0
|
HD2
|
B:LYS504
|
4.8
|
82.8
|
1.0
|
C
|
B:CYS499
|
4.9
|
55.0
|
1.0
|
N
|
B:LEU501
|
4.9
|
55.0
|
1.0
|
C
|
B:CYS502
|
5.0
|
53.4
|
1.0
|
NH2
|
B:ARG506
|
5.0
|
92.6
|
1.0
|
CA
|
B:LEU501
|
5.0
|
56.5
|
1.0
|
HA
|
B:CYS502
|
5.0
|
67.0
|
1.0
|
|
Reference:
C.H.Douse,
S.Bloor,
Y.Liu,
M.Shamin,
I.A.Tchasovnikarova,
R.T.Timms,
P.J.Lehner,
Y.Modis.
Neuropathic MORC2 Mutations Perturb Ghkl Atpase Dimerization Dynamics and Epigenetic Silencing By Multiple Structural Mechanisms. Nat Commun V. 9 651 2018.
ISSN: ESSN 2041-1723
PubMed: 29440755
DOI: 10.1038/S41467-018-03045-X
Page generated: Sun Oct 27 23:28:29 2024
|