Zinc in PDB 6az0: Mitochondrial Atpase Protease YME1
Other elements in 6az0:
The structure of Mitochondrial Atpase Protease YME1 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Mitochondrial Atpase Protease YME1
(pdb code 6az0). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
Mitochondrial Atpase Protease YME1, PDB code: 6az0:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 6az0
Go back to
Zinc Binding Sites List in 6az0
Zinc binding site 1 out
of 6 in the Mitochondrial Atpase Protease YME1
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Mitochondrial Atpase Protease YME1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn802
b:64.2
occ:1.00
|
OD2
|
A:ASP618
|
2.1
|
38.2
|
1.0
|
NE2
|
A:HIS544
|
2.2
|
36.8
|
1.0
|
NE2
|
A:HIS540
|
2.2
|
39.3
|
1.0
|
OD1
|
A:ASP618
|
2.6
|
38.2
|
1.0
|
CG
|
A:ASP618
|
2.7
|
38.2
|
1.0
|
CE1
|
A:HIS544
|
3.1
|
36.8
|
1.0
|
CD2
|
A:HIS544
|
3.1
|
36.8
|
1.0
|
CE1
|
A:HIS540
|
3.1
|
39.3
|
1.0
|
CD2
|
A:HIS540
|
3.2
|
39.3
|
1.0
|
ND1
|
A:HIS544
|
4.1
|
36.8
|
1.0
|
CG
|
A:HIS544
|
4.2
|
36.8
|
1.0
|
CB
|
A:ASP618
|
4.2
|
38.2
|
1.0
|
ND1
|
A:HIS540
|
4.3
|
39.3
|
1.0
|
CG
|
A:HIS540
|
4.4
|
39.3
|
1.0
|
|
Zinc binding site 2 out
of 6 in 6az0
Go back to
Zinc Binding Sites List in 6az0
Zinc binding site 2 out
of 6 in the Mitochondrial Atpase Protease YME1
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Mitochondrial Atpase Protease YME1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn802
b:89.8
occ:1.00
|
OD2
|
B:ASP618
|
2.0
|
41.6
|
1.0
|
NE2
|
B:HIS544
|
2.1
|
42.2
|
1.0
|
NE2
|
B:HIS540
|
2.2
|
48.0
|
1.0
|
OD1
|
B:ASP618
|
2.5
|
41.6
|
1.0
|
CG
|
B:ASP618
|
2.6
|
41.6
|
1.0
|
CE1
|
B:HIS540
|
2.7
|
48.0
|
1.0
|
CE1
|
B:HIS544
|
2.9
|
42.2
|
1.0
|
CD2
|
B:HIS544
|
3.3
|
42.2
|
1.0
|
CD2
|
B:HIS540
|
3.4
|
48.0
|
1.0
|
ND1
|
B:HIS540
|
3.9
|
48.0
|
1.0
|
CB
|
B:ASP618
|
4.1
|
41.6
|
1.0
|
ND1
|
B:HIS544
|
4.1
|
42.2
|
1.0
|
CG
|
B:HIS544
|
4.3
|
42.2
|
1.0
|
CG
|
B:HIS540
|
4.3
|
48.0
|
1.0
|
CA
|
B:GLY598
|
4.7
|
44.7
|
1.0
|
O
|
B:GLY614
|
5.0
|
48.5
|
1.0
|
CA
|
B:ASP618
|
5.0
|
41.6
|
1.0
|
|
Zinc binding site 3 out
of 6 in 6az0
Go back to
Zinc Binding Sites List in 6az0
Zinc binding site 3 out
of 6 in the Mitochondrial Atpase Protease YME1
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Mitochondrial Atpase Protease YME1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn802
b:72.0
occ:1.00
|
OD2
|
C:ASP618
|
2.0
|
40.0
|
1.0
|
NE2
|
C:HIS540
|
2.2
|
45.2
|
1.0
|
NE2
|
C:HIS544
|
2.2
|
42.7
|
1.0
|
OD1
|
C:ASP618
|
2.4
|
40.0
|
1.0
|
CG
|
C:ASP618
|
2.5
|
40.0
|
1.0
|
CE1
|
C:HIS540
|
3.0
|
45.2
|
1.0
|
CE1
|
C:HIS544
|
3.0
|
42.7
|
1.0
|
CD2
|
C:HIS540
|
3.2
|
45.2
|
1.0
|
CD2
|
C:HIS544
|
3.2
|
42.7
|
1.0
|
CB
|
C:ASP618
|
4.0
|
40.0
|
1.0
|
ND1
|
C:HIS544
|
4.2
|
42.7
|
1.0
|
ND1
|
C:HIS540
|
4.2
|
45.2
|
1.0
|
CG
|
C:HIS540
|
4.2
|
45.2
|
1.0
|
CG
|
C:HIS544
|
4.3
|
42.7
|
1.0
|
CA
|
C:ASP618
|
4.9
|
40.0
|
1.0
|
|
Zinc binding site 4 out
of 6 in 6az0
Go back to
Zinc Binding Sites List in 6az0
Zinc binding site 4 out
of 6 in the Mitochondrial Atpase Protease YME1
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Mitochondrial Atpase Protease YME1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn801
b:75.4
occ:1.00
|
OD2
|
D:ASP618
|
2.0
|
45.5
|
1.0
|
NE2
|
D:HIS544
|
2.1
|
48.4
|
1.0
|
NE2
|
D:HIS540
|
2.1
|
53.4
|
1.0
|
CE1
|
D:HIS540
|
3.0
|
53.4
|
1.0
|
CE1
|
D:HIS544
|
3.1
|
48.4
|
1.0
|
CD2
|
D:HIS544
|
3.1
|
48.4
|
1.0
|
CG
|
D:ASP618
|
3.1
|
45.5
|
1.0
|
CD2
|
D:HIS540
|
3.2
|
53.4
|
1.0
|
CB
|
D:ASP618
|
3.8
|
45.5
|
1.0
|
OD1
|
D:ASP618
|
4.0
|
45.5
|
1.0
|
ND1
|
D:HIS540
|
4.2
|
53.4
|
1.0
|
ND1
|
D:HIS544
|
4.2
|
48.4
|
1.0
|
CG
|
D:HIS544
|
4.2
|
48.4
|
1.0
|
CG
|
D:HIS540
|
4.2
|
53.4
|
1.0
|
CA
|
D:GLY598
|
5.0
|
51.2
|
1.0
|
|
Zinc binding site 5 out
of 6 in 6az0
Go back to
Zinc Binding Sites List in 6az0
Zinc binding site 5 out
of 6 in the Mitochondrial Atpase Protease YME1
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Mitochondrial Atpase Protease YME1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn802
b:45.0
occ:1.00
|
OD2
|
E:ASP618
|
2.0
|
43.6
|
1.0
|
NE2
|
E:HIS540
|
2.1
|
51.6
|
1.0
|
NE2
|
E:HIS544
|
2.2
|
47.0
|
1.0
|
OD1
|
E:ASP618
|
2.4
|
43.6
|
1.0
|
CG
|
E:ASP618
|
2.5
|
43.6
|
1.0
|
CE1
|
E:HIS540
|
2.6
|
51.6
|
1.0
|
CE1
|
E:HIS544
|
3.0
|
47.0
|
1.0
|
CD2
|
E:HIS544
|
3.3
|
47.0
|
1.0
|
CD2
|
E:HIS540
|
3.4
|
51.6
|
1.0
|
ND1
|
E:HIS540
|
3.9
|
51.6
|
1.0
|
CB
|
E:ASP618
|
4.0
|
43.6
|
1.0
|
ND1
|
E:HIS544
|
4.1
|
47.0
|
1.0
|
CG
|
E:HIS540
|
4.3
|
51.6
|
1.0
|
CG
|
E:HIS544
|
4.3
|
47.0
|
1.0
|
CA
|
E:GLY598
|
4.9
|
46.9
|
1.0
|
CA
|
E:ASP618
|
4.9
|
43.6
|
1.0
|
|
Zinc binding site 6 out
of 6 in 6az0
Go back to
Zinc Binding Sites List in 6az0
Zinc binding site 6 out
of 6 in the Mitochondrial Atpase Protease YME1
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Mitochondrial Atpase Protease YME1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Zn801
b:0.8
occ:1.00
|
OD2
|
F:ASP618
|
1.7
|
56.5
|
1.0
|
NE2
|
F:HIS540
|
2.1
|
59.7
|
1.0
|
CG
|
F:ASP618
|
2.5
|
56.5
|
1.0
|
NE2
|
F:HIS544
|
2.6
|
57.1
|
1.0
|
CE1
|
F:HIS540
|
2.7
|
59.7
|
1.0
|
OD1
|
F:ASP618
|
2.7
|
56.5
|
1.0
|
CD2
|
F:HIS540
|
3.3
|
59.7
|
1.0
|
CE1
|
F:HIS544
|
3.5
|
57.1
|
1.0
|
CD2
|
F:HIS544
|
3.5
|
57.1
|
1.0
|
CB
|
F:ASP618
|
3.9
|
56.5
|
1.0
|
ND1
|
F:HIS540
|
3.9
|
59.7
|
1.0
|
CG
|
F:HIS540
|
4.3
|
59.7
|
1.0
|
ND1
|
F:HIS544
|
4.6
|
57.1
|
1.0
|
CG
|
F:HIS544
|
4.6
|
57.1
|
1.0
|
CA
|
F:ASP618
|
5.0
|
56.5
|
1.0
|
|
Reference:
C.Puchades,
A.J.Rampello,
M.Shin,
C.J.Giuliano,
R.L.Wiseman,
S.E.Glynn,
G.C.Lander.
Structure of the Mitochondrial Inner Membrane Aaa+ Protease YME1 Gives Insight Into Substrate Processing. Science V. 358 2017.
ISSN: ESSN 1095-9203
PubMed: 29097521
DOI: 10.1126/SCIENCE.AAO0464
Page generated: Mon Oct 28 17:45:58 2024
|