Manganese in PDB 5f13: Structure of Mn Bound DUF89 From Saccharomyces Cerevisiae
Protein crystallography data
The structure of Structure of Mn Bound DUF89 From Saccharomyces Cerevisiae, PDB code: 5f13
was solved by
B.Nocek,
T.Skarina,
A.Joachimiak,
A.Savchenko,
A.Yakunin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.17 /
2.39
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
223.035,
95.550,
78.097,
90.00,
105.84,
90.00
|
R / Rfree (%)
|
19.9 /
23.7
|
Other elements in 5f13:
The structure of Structure of Mn Bound DUF89 From Saccharomyces Cerevisiae also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Structure of Mn Bound DUF89 From Saccharomyces Cerevisiae
(pdb code 5f13). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the
Structure of Mn Bound DUF89 From Saccharomyces Cerevisiae, PDB code: 5f13:
Jump to Manganese binding site number:
1;
2;
3;
Manganese binding site 1 out
of 3 in 5f13
Go back to
Manganese Binding Sites List in 5f13
Manganese binding site 1 out
of 3 in the Structure of Mn Bound DUF89 From Saccharomyces Cerevisiae
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Structure of Mn Bound DUF89 From Saccharomyces Cerevisiae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn501
b:33.0
occ:0.94
|
OD1
|
A:ASP292
|
2.3
|
21.1
|
1.0
|
O
|
A:HOH632
|
2.3
|
29.5
|
1.0
|
O1
|
A:PO4502
|
2.3
|
42.4
|
1.0
|
OD1
|
A:ASP254
|
2.4
|
24.4
|
1.0
|
O
|
A:HOH636
|
2.5
|
29.8
|
1.0
|
OD1
|
A:ASN255
|
2.6
|
28.1
|
1.0
|
HD21
|
A:ASN255
|
3.1
|
33.2
|
1.0
|
O3
|
A:PO4502
|
3.1
|
42.1
|
1.0
|
CG
|
A:ASN255
|
3.2
|
27.5
|
1.0
|
P
|
A:PO4502
|
3.3
|
42.4
|
1.0
|
CG
|
A:ASP254
|
3.4
|
24.4
|
1.0
|
CG
|
A:ASP292
|
3.4
|
19.9
|
1.0
|
ND2
|
A:ASN255
|
3.4
|
27.7
|
1.0
|
HG
|
A:SER291
|
3.6
|
29.5
|
1.0
|
HB3
|
A:MET289
|
3.7
|
30.9
|
1.0
|
OD2
|
A:ASP254
|
3.8
|
25.6
|
1.0
|
OD2
|
A:ASP292
|
3.9
|
18.8
|
1.0
|
HB2
|
A:MET289
|
3.9
|
30.9
|
1.0
|
HD22
|
A:ASN255
|
4.1
|
33.2
|
1.0
|
HA
|
A:ASN255
|
4.2
|
29.6
|
1.0
|
O2
|
A:PO4502
|
4.2
|
42.7
|
1.0
|
O
|
A:HOH627
|
4.2
|
43.0
|
1.0
|
CB
|
A:MET289
|
4.3
|
25.7
|
1.0
|
HA
|
A:ASP292
|
4.3
|
25.6
|
1.0
|
N
|
A:ASN255
|
4.3
|
23.4
|
1.0
|
OG
|
A:SER291
|
4.3
|
24.6
|
1.0
|
O4
|
A:PO4502
|
4.4
|
40.3
|
1.0
|
CB
|
A:ASN255
|
4.4
|
26.8
|
1.0
|
H
|
A:ASN255
|
4.4
|
28.1
|
1.0
|
C
|
A:ASP254
|
4.5
|
23.1
|
1.0
|
O
|
A:MET289
|
4.5
|
31.1
|
1.0
|
CA
|
A:ASN255
|
4.5
|
24.7
|
1.0
|
HG3
|
A:MET289
|
4.6
|
28.9
|
1.0
|
HA
|
A:ASP254
|
4.6
|
27.1
|
1.0
|
CB
|
A:ASP292
|
4.6
|
20.1
|
1.0
|
O2
|
A:PO4503
|
4.6
|
38.7
|
1.0
|
O
|
A:HOH649
|
4.7
|
30.4
|
1.0
|
CB
|
A:ASP254
|
4.7
|
23.4
|
1.0
|
N
|
A:ASP292
|
4.7
|
23.8
|
1.0
|
CA
|
A:ASP292
|
4.8
|
21.3
|
1.0
|
H
|
A:ASP292
|
4.8
|
28.6
|
1.0
|
H
|
A:SER291
|
4.8
|
29.6
|
1.0
|
CA
|
A:ASP254
|
4.8
|
22.6
|
1.0
|
O
|
A:ASP254
|
4.8
|
22.7
|
1.0
|
HB3
|
A:ASN255
|
4.9
|
32.1
|
1.0
|
|
Manganese binding site 2 out
of 3 in 5f13
Go back to
Manganese Binding Sites List in 5f13
Manganese binding site 2 out
of 3 in the Structure of Mn Bound DUF89 From Saccharomyces Cerevisiae
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Structure of Mn Bound DUF89 From Saccharomyces Cerevisiae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn501
b:38.6
occ:0.90
|
O1
|
B:PO4502
|
2.1
|
49.9
|
1.0
|
OD1
|
B:ASP254
|
2.2
|
32.7
|
1.0
|
O
|
B:HOH608
|
2.2
|
34.1
|
1.0
|
OD1
|
B:ASN255
|
2.2
|
28.7
|
1.0
|
OD1
|
B:ASP292
|
2.3
|
29.2
|
1.0
|
O
|
B:HOH628
|
2.3
|
27.9
|
1.0
|
P
|
B:PO4502
|
3.2
|
48.2
|
1.0
|
CG
|
B:ASN255
|
3.2
|
28.7
|
1.0
|
O3
|
B:PO4502
|
3.2
|
46.4
|
1.0
|
CG
|
B:ASP254
|
3.2
|
32.7
|
1.0
|
HD21
|
B:ASN255
|
3.3
|
34.7
|
1.0
|
CG
|
B:ASP292
|
3.4
|
29.0
|
1.0
|
OD2
|
B:ASP254
|
3.6
|
33.1
|
1.0
|
ND2
|
B:ASN255
|
3.6
|
28.9
|
1.0
|
HB3
|
B:MET289
|
3.7
|
43.0
|
1.0
|
OD2
|
B:ASP292
|
3.8
|
29.3
|
1.0
|
HB2
|
B:MET289
|
3.9
|
43.0
|
1.0
|
HG
|
B:SER291
|
3.9
|
43.6
|
1.0
|
O
|
B:HOH603
|
4.0
|
30.4
|
1.0
|
O4
|
B:PO4502
|
4.0
|
49.5
|
1.0
|
CB
|
B:MET289
|
4.2
|
35.9
|
1.0
|
HA
|
B:ASN255
|
4.2
|
33.4
|
1.0
|
N
|
B:ASN255
|
4.3
|
27.4
|
1.0
|
HA
|
B:ASP292
|
4.3
|
35.0
|
1.0
|
O2
|
B:PO4502
|
4.3
|
52.1
|
1.0
|
HG3
|
B:MET289
|
4.3
|
43.1
|
1.0
|
C
|
B:ASP254
|
4.4
|
31.8
|
1.0
|
H
|
B:ASN255
|
4.4
|
32.9
|
1.0
|
CB
|
B:ASN255
|
4.5
|
28.7
|
1.0
|
HA
|
B:ASP254
|
4.5
|
38.4
|
1.0
|
HD22
|
B:ASN255
|
4.5
|
34.7
|
1.0
|
CB
|
B:ASP254
|
4.5
|
32.4
|
1.0
|
CA
|
B:ASN255
|
4.6
|
27.9
|
1.0
|
O1
|
B:PO4503
|
4.6
|
57.2
|
1.0
|
O
|
B:MET289
|
4.6
|
37.3
|
1.0
|
OG
|
B:SER291
|
4.6
|
36.3
|
1.0
|
CB
|
B:ASP292
|
4.6
|
28.8
|
1.0
|
CA
|
B:ASP254
|
4.7
|
32.0
|
1.0
|
O
|
B:ASP254
|
4.8
|
31.8
|
1.0
|
CA
|
B:ASP292
|
4.8
|
29.1
|
1.0
|
N
|
B:ASP292
|
4.8
|
30.1
|
1.0
|
CG
|
B:MET289
|
4.8
|
35.9
|
1.0
|
H
|
B:ASP292
|
4.9
|
36.1
|
1.0
|
O
|
B:HOH634
|
5.0
|
39.0
|
1.0
|
HB3
|
B:ASN255
|
5.0
|
34.4
|
1.0
|
H
|
B:SER291
|
5.0
|
43.5
|
1.0
|
|
Manganese binding site 3 out
of 3 in 5f13
Go back to
Manganese Binding Sites List in 5f13
Manganese binding site 3 out
of 3 in the Structure of Mn Bound DUF89 From Saccharomyces Cerevisiae
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Structure of Mn Bound DUF89 From Saccharomyces Cerevisiae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn501
b:48.6
occ:0.96
|
O2
|
C:PO4502
|
2.1
|
70.6
|
1.0
|
O
|
C:HOH609
|
2.1
|
39.2
|
1.0
|
OD1
|
C:ASP292
|
2.3
|
46.1
|
1.0
|
O
|
C:HOH608
|
2.3
|
35.3
|
1.0
|
OD1
|
C:ASN255
|
2.3
|
49.4
|
1.0
|
OD1
|
C:ASP254
|
2.4
|
46.8
|
1.0
|
CG
|
C:ASN255
|
3.0
|
50.0
|
1.0
|
HD21
|
C:ASN255
|
3.1
|
60.1
|
1.0
|
CG
|
C:ASP254
|
3.3
|
47.7
|
1.0
|
ND2
|
C:ASN255
|
3.3
|
50.1
|
1.0
|
P
|
C:PO4502
|
3.4
|
68.9
|
1.0
|
CG
|
C:ASP292
|
3.4
|
45.1
|
1.0
|
O4
|
C:PO4502
|
3.5
|
64.5
|
1.0
|
OD2
|
C:ASP254
|
3.7
|
48.8
|
1.0
|
HB3
|
C:MET289
|
3.7
|
49.9
|
1.0
|
HG
|
C:SER291
|
3.7
|
53.5
|
1.0
|
HB2
|
C:MET289
|
3.8
|
49.9
|
1.0
|
OD2
|
C:ASP292
|
4.0
|
44.1
|
1.0
|
HA
|
C:ASN255
|
4.0
|
59.4
|
1.0
|
HD22
|
C:ASN255
|
4.1
|
60.1
|
1.0
|
N
|
C:ASN255
|
4.1
|
48.6
|
1.0
|
HA
|
C:ASP292
|
4.2
|
55.6
|
1.0
|
CB
|
C:MET289
|
4.2
|
41.6
|
1.0
|
CB
|
C:ASN255
|
4.2
|
50.7
|
1.0
|
O3
|
C:PO4502
|
4.2
|
68.3
|
1.0
|
H
|
C:ASN255
|
4.3
|
58.4
|
1.0
|
C
|
C:ASP254
|
4.3
|
49.0
|
1.0
|
CA
|
C:ASN255
|
4.4
|
49.5
|
1.0
|
O
|
C:MET289
|
4.4
|
43.9
|
1.0
|
O1
|
C:PO4502
|
4.4
|
72.2
|
1.0
|
OG
|
C:SER291
|
4.4
|
44.6
|
1.0
|
HA
|
C:ASP254
|
4.5
|
58.0
|
1.0
|
HG3
|
C:MET289
|
4.6
|
48.8
|
1.0
|
CB
|
C:ASP254
|
4.6
|
47.6
|
1.0
|
CB
|
C:ASP292
|
4.6
|
45.1
|
1.0
|
HB3
|
C:ASN255
|
4.7
|
60.8
|
1.0
|
O
|
C:ASP254
|
4.7
|
48.4
|
1.0
|
O3
|
C:PO4503
|
4.7
|
75.1
|
1.0
|
CA
|
C:ASP254
|
4.7
|
48.4
|
1.0
|
N
|
C:ASP292
|
4.7
|
46.9
|
1.0
|
CA
|
C:ASP292
|
4.7
|
46.4
|
1.0
|
H
|
C:SER291
|
4.8
|
51.2
|
1.0
|
H
|
C:ASP292
|
4.8
|
56.2
|
1.0
|
HB2
|
C:ASN255
|
4.9
|
60.8
|
1.0
|
HB2
|
C:ASP292
|
4.9
|
54.1
|
1.0
|
CG
|
C:MET289
|
5.0
|
40.7
|
1.0
|
C
|
C:SER291
|
5.0
|
42.7
|
1.0
|
|
Reference:
L.Huang,
A.Khusnutdinova,
B.Nocek,
G.Brown,
X.Xu,
H.Cui,
P.Petit,
R.Flick,
R.Zallot,
K.Balmant,
M.J.Ziemak,
J.Shanklin,
V.De Crecy-Lagard,
O.Fiehn,
J.F.Gregory,
A.Joachimiak,
A.Savchenko,
A.F.Yakunin,
A.D.Hanson.
A Family of Metal-Dependent Phosphatases Implicated in Metabolite Damage-Control. Nat.Chem.Biol. V. 12 621 2016.
ISSN: ESSN 1552-4469
PubMed: 27322068
DOI: 10.1038/NCHEMBIO.2108
Page generated: Sun Oct 6 00:10:29 2024
|