Zinc in PDB 1hi9: Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
Protein crystallography data
The structure of Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease., PDB code: 1hi9
was solved by
H.Remaut,
C.Bompard-Gilles,
C.Goffin,
J.M.Frere,
J.Van Beeumen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
15.00 /
2.40
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
145.110,
165.860,
109.930,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
23.2 /
26.8
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
(pdb code 1hi9). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 10 binding sites of Zinc where determined in the
Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease., PDB code: 1hi9:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Zinc binding site 1 out
of 10 in 1hi9
Go back to
Zinc Binding Sites List in 1hi9
Zinc binding site 1 out
of 10 in the Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn300
b:31.8
occ:1.00
|
NE2
|
A:HIS104
|
1.9
|
31.5
|
1.0
|
OE1
|
A:GLU133
|
2.0
|
33.4
|
1.0
|
OD2
|
A:ASP8
|
2.0
|
36.5
|
1.0
|
O
|
A:HOH2059
|
2.1
|
28.8
|
1.0
|
CD
|
A:GLU133
|
2.7
|
33.1
|
1.0
|
OE2
|
A:GLU133
|
2.7
|
30.9
|
1.0
|
CE1
|
A:HIS104
|
2.9
|
26.9
|
1.0
|
CD2
|
A:HIS104
|
2.9
|
29.8
|
1.0
|
CG
|
A:ASP8
|
3.1
|
35.7
|
1.0
|
ZN
|
A:ZN301
|
3.1
|
56.2
|
1.0
|
OD1
|
A:ASP8
|
3.5
|
37.2
|
1.0
|
NE2
|
A:HIS115
|
3.6
|
36.5
|
1.0
|
OE1
|
A:GLU10
|
3.8
|
35.2
|
1.0
|
CE1
|
A:HIS115
|
3.9
|
35.5
|
1.0
|
ND1
|
A:HIS104
|
4.0
|
30.6
|
1.0
|
CG
|
A:HIS104
|
4.0
|
29.9
|
1.0
|
CG
|
A:GLU133
|
4.1
|
33.5
|
1.0
|
CE
|
A:MET87
|
4.2
|
32.1
|
1.0
|
CB
|
A:ASP8
|
4.4
|
36.0
|
1.0
|
CD
|
A:GLU10
|
4.5
|
34.9
|
1.0
|
CD2
|
A:HIS115
|
4.5
|
34.4
|
1.0
|
CB
|
A:GLU133
|
4.7
|
35.0
|
1.0
|
OE2
|
A:GLU10
|
4.8
|
36.7
|
1.0
|
SD
|
A:MET87
|
4.8
|
34.5
|
1.0
|
ND1
|
A:HIS115
|
5.0
|
34.7
|
1.0
|
|
Zinc binding site 2 out
of 10 in 1hi9
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Zinc Binding Sites List in 1hi9
Zinc binding site 2 out
of 10 in the Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:56.2
occ:1.00
|
OD1
|
A:ASP8
|
2.3
|
37.2
|
1.0
|
OE1
|
A:GLU10
|
2.3
|
35.2
|
1.0
|
ND1
|
A:HIS60
|
2.5
|
36.0
|
1.0
|
O
|
A:HOH2059
|
2.5
|
28.8
|
1.0
|
OE2
|
A:GLU10
|
2.8
|
36.7
|
1.0
|
CD
|
A:GLU10
|
2.9
|
34.9
|
1.0
|
CG
|
A:ASP8
|
3.1
|
35.7
|
1.0
|
ZN
|
A:ZN300
|
3.1
|
31.8
|
1.0
|
OD2
|
A:ASP8
|
3.2
|
36.5
|
1.0
|
CE1
|
A:HIS60
|
3.3
|
35.3
|
1.0
|
CG
|
A:HIS60
|
3.6
|
36.5
|
1.0
|
CB
|
A:HIS60
|
3.9
|
36.0
|
1.0
|
CA
|
A:HIS60
|
4.1
|
36.4
|
1.0
|
NE2
|
A:HIS115
|
4.1
|
36.5
|
1.0
|
NE2
|
A:HIS104
|
4.2
|
31.5
|
1.0
|
N
|
A:MET9
|
4.2
|
33.4
|
1.0
|
CG
|
A:GLU10
|
4.4
|
35.8
|
1.0
|
CE1
|
A:HIS115
|
4.4
|
35.5
|
1.0
|
CB
|
A:ASP8
|
4.4
|
36.0
|
1.0
|
CD2
|
A:HIS104
|
4.5
|
29.8
|
1.0
|
NE2
|
A:HIS60
|
4.5
|
35.4
|
1.0
|
N
|
A:SER61
|
4.6
|
37.3
|
1.0
|
N
|
A:GLU10
|
4.6
|
30.6
|
1.0
|
O
|
A:SER59
|
4.6
|
37.6
|
1.0
|
CD2
|
A:HIS60
|
4.7
|
35.8
|
1.0
|
OE1
|
A:GLU133
|
4.8
|
33.4
|
1.0
|
C
|
A:HIS60
|
4.9
|
36.7
|
1.0
|
CA
|
A:ASP8
|
4.9
|
35.1
|
1.0
|
CB
|
A:GLU10
|
5.0
|
32.9
|
1.0
|
CB
|
A:MET9
|
5.0
|
32.9
|
1.0
|
O
|
A:HOH2001
|
5.0
|
39.8
|
1.0
|
|
Zinc binding site 3 out
of 10 in 1hi9
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Zinc Binding Sites List in 1hi9
Zinc binding site 3 out
of 10 in the Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn300
b:40.5
occ:1.00
|
OE1
|
B:GLU133
|
2.0
|
36.5
|
1.0
|
NE2
|
B:HIS104
|
2.0
|
35.3
|
1.0
|
OD2
|
B:ASP8
|
2.0
|
28.2
|
1.0
|
O
|
B:HOH2025
|
2.1
|
32.5
|
1.0
|
CD
|
B:GLU133
|
2.6
|
35.9
|
1.0
|
OE2
|
B:GLU133
|
2.7
|
35.8
|
1.0
|
CD2
|
B:HIS104
|
2.9
|
33.2
|
1.0
|
CE1
|
B:HIS104
|
2.9
|
33.8
|
1.0
|
CG
|
B:ASP8
|
3.1
|
35.6
|
1.0
|
ZN
|
B:ZN301
|
3.2
|
63.7
|
1.0
|
OD1
|
B:ASP8
|
3.5
|
39.2
|
1.0
|
NE2
|
B:HIS115
|
3.6
|
38.9
|
1.0
|
O
|
B:HOH2009
|
3.6
|
36.9
|
1.0
|
OE1
|
B:GLU10
|
3.8
|
38.3
|
1.0
|
CE1
|
B:HIS115
|
4.0
|
39.5
|
1.0
|
ND1
|
B:HIS104
|
4.0
|
35.3
|
1.0
|
CG
|
B:HIS104
|
4.1
|
34.5
|
1.0
|
CG
|
B:GLU133
|
4.1
|
38.2
|
1.0
|
CE
|
B:MET87
|
4.1
|
34.2
|
1.0
|
CB
|
B:ASP8
|
4.4
|
37.8
|
1.0
|
CD2
|
B:HIS115
|
4.5
|
39.2
|
1.0
|
CD
|
B:GLU10
|
4.6
|
37.5
|
1.0
|
CB
|
B:GLU133
|
4.6
|
39.1
|
1.0
|
SD
|
B:MET87
|
4.7
|
42.1
|
1.0
|
OE2
|
B:GLU10
|
4.9
|
38.8
|
1.0
|
|
Zinc binding site 4 out
of 10 in 1hi9
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Zinc Binding Sites List in 1hi9
Zinc binding site 4 out
of 10 in the Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn301
b:63.7
occ:1.00
|
OE1
|
B:GLU10
|
2.3
|
38.3
|
1.0
|
OD1
|
B:ASP8
|
2.3
|
39.2
|
1.0
|
ND1
|
B:HIS60
|
2.5
|
37.5
|
1.0
|
O
|
B:HOH2025
|
2.6
|
32.5
|
1.0
|
OE2
|
B:GLU10
|
2.8
|
38.8
|
1.0
|
CD
|
B:GLU10
|
2.9
|
37.5
|
1.0
|
CG
|
B:ASP8
|
3.0
|
35.6
|
1.0
|
OD2
|
B:ASP8
|
3.1
|
28.2
|
1.0
|
ZN
|
B:ZN300
|
3.2
|
40.5
|
1.0
|
CE1
|
B:HIS60
|
3.3
|
39.1
|
1.0
|
CG
|
B:HIS60
|
3.6
|
38.7
|
1.0
|
CB
|
B:HIS60
|
4.0
|
39.6
|
1.0
|
NE2
|
B:HIS115
|
4.1
|
38.9
|
1.0
|
NE2
|
B:HIS104
|
4.1
|
35.3
|
1.0
|
CA
|
B:HIS60
|
4.2
|
39.1
|
1.0
|
N
|
B:MET9
|
4.3
|
37.9
|
1.0
|
CE1
|
B:HIS115
|
4.4
|
39.5
|
1.0
|
CG
|
B:GLU10
|
4.4
|
36.6
|
1.0
|
CB
|
B:ASP8
|
4.4
|
37.8
|
1.0
|
CD2
|
B:HIS104
|
4.4
|
33.2
|
1.0
|
NE2
|
B:HIS60
|
4.5
|
40.3
|
1.0
|
N
|
B:GLU10
|
4.6
|
34.4
|
1.0
|
N
|
B:SER61
|
4.6
|
40.4
|
1.0
|
CD2
|
B:HIS60
|
4.7
|
38.9
|
1.0
|
O
|
B:SER59
|
4.7
|
41.6
|
1.0
|
OE1
|
B:GLU133
|
4.8
|
36.5
|
1.0
|
C
|
B:HIS60
|
4.9
|
38.7
|
1.0
|
CA
|
B:ASP8
|
4.9
|
37.9
|
1.0
|
CB
|
B:GLU10
|
5.0
|
34.0
|
1.0
|
|
Zinc binding site 5 out
of 10 in 1hi9
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Zinc Binding Sites List in 1hi9
Zinc binding site 5 out
of 10 in the Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn300
b:42.7
occ:1.00
|
OD2
|
C:ASP8
|
2.0
|
31.4
|
1.0
|
NE2
|
C:HIS104
|
2.0
|
34.7
|
1.0
|
OE1
|
C:GLU133
|
2.0
|
38.8
|
1.0
|
O
|
C:HOH2037
|
2.1
|
32.2
|
1.0
|
CD
|
C:GLU133
|
2.6
|
37.0
|
1.0
|
OE2
|
C:GLU133
|
2.7
|
37.9
|
1.0
|
CD2
|
C:HIS104
|
2.9
|
33.2
|
1.0
|
CE1
|
C:HIS104
|
2.9
|
35.7
|
1.0
|
CG
|
C:ASP8
|
3.1
|
37.3
|
1.0
|
ZN
|
C:ZN301
|
3.2
|
60.2
|
1.0
|
OD1
|
C:ASP8
|
3.5
|
39.2
|
1.0
|
NE2
|
C:HIS115
|
3.6
|
42.4
|
1.0
|
OE1
|
C:GLU10
|
3.8
|
37.2
|
1.0
|
CE1
|
C:HIS115
|
4.0
|
41.9
|
1.0
|
ND1
|
C:HIS104
|
4.0
|
36.8
|
1.0
|
CG
|
C:HIS104
|
4.1
|
34.9
|
1.0
|
CG
|
C:GLU133
|
4.1
|
38.1
|
1.0
|
CE
|
C:MET87
|
4.1
|
34.8
|
1.0
|
CB
|
C:ASP8
|
4.4
|
36.4
|
1.0
|
CD
|
C:GLU10
|
4.5
|
37.8
|
1.0
|
CD2
|
C:HIS115
|
4.6
|
39.5
|
1.0
|
CB
|
C:GLU133
|
4.6
|
38.8
|
1.0
|
SD
|
C:MET87
|
4.7
|
37.7
|
1.0
|
OE2
|
C:GLU10
|
4.9
|
38.8
|
1.0
|
|
Zinc binding site 6 out
of 10 in 1hi9
Go back to
Zinc Binding Sites List in 1hi9
Zinc binding site 6 out
of 10 in the Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn301
b:60.2
occ:1.00
|
OD1
|
C:ASP8
|
2.3
|
39.2
|
1.0
|
OE1
|
C:GLU10
|
2.4
|
37.2
|
1.0
|
ND1
|
C:HIS60
|
2.5
|
37.1
|
1.0
|
O
|
C:HOH2037
|
2.6
|
32.2
|
1.0
|
OE2
|
C:GLU10
|
2.9
|
38.8
|
1.0
|
CD
|
C:GLU10
|
3.0
|
37.8
|
1.0
|
CG
|
C:ASP8
|
3.1
|
37.3
|
1.0
|
OD2
|
C:ASP8
|
3.2
|
31.4
|
1.0
|
ZN
|
C:ZN300
|
3.2
|
42.7
|
1.0
|
CE1
|
C:HIS60
|
3.3
|
36.8
|
1.0
|
CG
|
C:HIS60
|
3.5
|
36.5
|
1.0
|
CB
|
C:HIS60
|
3.9
|
39.2
|
1.0
|
CA
|
C:HIS60
|
4.1
|
39.2
|
1.0
|
NE2
|
C:HIS115
|
4.2
|
42.4
|
1.0
|
NE2
|
C:HIS104
|
4.2
|
34.7
|
1.0
|
N
|
C:MET9
|
4.3
|
36.0
|
1.0
|
CB
|
C:ASP8
|
4.4
|
36.4
|
1.0
|
CE1
|
C:HIS115
|
4.5
|
41.9
|
1.0
|
CG
|
C:GLU10
|
4.5
|
37.3
|
1.0
|
NE2
|
C:HIS60
|
4.5
|
37.6
|
1.0
|
N
|
C:SER61
|
4.5
|
40.7
|
1.0
|
CD2
|
C:HIS104
|
4.5
|
33.2
|
1.0
|
O
|
C:SER59
|
4.6
|
37.1
|
1.0
|
CD2
|
C:HIS60
|
4.6
|
38.2
|
1.0
|
N
|
C:GLU10
|
4.6
|
35.2
|
1.0
|
C
|
C:HIS60
|
4.8
|
40.4
|
1.0
|
OE1
|
C:GLU133
|
4.9
|
38.8
|
1.0
|
CA
|
C:ASP8
|
4.9
|
36.3
|
1.0
|
CB
|
C:MET9
|
5.0
|
38.1
|
1.0
|
|
Zinc binding site 7 out
of 10 in 1hi9
Go back to
Zinc Binding Sites List in 1hi9
Zinc binding site 7 out
of 10 in the Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn300
b:33.5
occ:1.00
|
OE1
|
D:GLU133
|
1.9
|
35.7
|
1.0
|
NE2
|
D:HIS104
|
2.0
|
26.6
|
1.0
|
OD2
|
D:ASP8
|
2.0
|
35.2
|
1.0
|
O
|
D:HOH2053
|
2.1
|
35.3
|
1.0
|
CD
|
D:GLU133
|
2.6
|
35.7
|
1.0
|
OE2
|
D:GLU133
|
2.6
|
35.8
|
1.0
|
CE1
|
D:HIS104
|
2.9
|
29.2
|
1.0
|
CD2
|
D:HIS104
|
3.0
|
26.0
|
1.0
|
CG
|
D:ASP8
|
3.1
|
36.5
|
1.0
|
ZN
|
D:ZN301
|
3.2
|
57.0
|
1.0
|
O
|
D:HOH2003
|
3.4
|
38.4
|
1.0
|
OD1
|
D:ASP8
|
3.5
|
38.5
|
1.0
|
NE2
|
D:HIS115
|
3.6
|
37.5
|
1.0
|
OE1
|
D:GLU10
|
3.9
|
34.6
|
1.0
|
CE1
|
D:HIS115
|
4.0
|
37.6
|
1.0
|
CG
|
D:GLU133
|
4.0
|
35.5
|
1.0
|
ND1
|
D:HIS104
|
4.0
|
26.4
|
1.0
|
CG
|
D:HIS104
|
4.1
|
28.5
|
1.0
|
CE
|
D:MET87
|
4.2
|
31.7
|
1.0
|
CB
|
D:ASP8
|
4.4
|
36.9
|
1.0
|
CD2
|
D:HIS115
|
4.6
|
37.4
|
1.0
|
CB
|
D:GLU133
|
4.6
|
35.4
|
1.0
|
CD
|
D:GLU10
|
4.6
|
35.5
|
1.0
|
SD
|
D:MET87
|
4.7
|
34.0
|
1.0
|
OE2
|
D:GLU10
|
4.9
|
37.3
|
1.0
|
ND1
|
D:HIS115
|
5.0
|
37.1
|
1.0
|
|
Zinc binding site 8 out
of 10 in 1hi9
Go back to
Zinc Binding Sites List in 1hi9
Zinc binding site 8 out
of 10 in the Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn301
b:57.0
occ:1.00
|
OE1
|
D:GLU10
|
2.3
|
34.6
|
1.0
|
OD1
|
D:ASP8
|
2.3
|
38.5
|
1.0
|
O
|
D:HOH2053
|
2.5
|
35.3
|
1.0
|
ND1
|
D:HIS60
|
2.5
|
34.9
|
1.0
|
OE2
|
D:GLU10
|
2.8
|
37.3
|
1.0
|
CD
|
D:GLU10
|
2.9
|
35.5
|
1.0
|
CG
|
D:ASP8
|
3.1
|
36.5
|
1.0
|
ZN
|
D:ZN300
|
3.2
|
33.5
|
1.0
|
OD2
|
D:ASP8
|
3.2
|
35.2
|
1.0
|
CE1
|
D:HIS60
|
3.4
|
34.0
|
1.0
|
CG
|
D:HIS60
|
3.6
|
32.9
|
1.0
|
CB
|
D:HIS60
|
4.0
|
34.3
|
1.0
|
NE2
|
D:HIS115
|
4.1
|
37.5
|
1.0
|
NE2
|
D:HIS104
|
4.1
|
26.6
|
1.0
|
CA
|
D:HIS60
|
4.2
|
35.0
|
1.0
|
N
|
D:MET9
|
4.3
|
36.1
|
1.0
|
CE1
|
D:HIS115
|
4.3
|
37.6
|
1.0
|
CG
|
D:GLU10
|
4.3
|
36.0
|
1.0
|
CD2
|
D:HIS104
|
4.4
|
26.0
|
1.0
|
CB
|
D:ASP8
|
4.5
|
36.9
|
1.0
|
NE2
|
D:HIS60
|
4.5
|
33.7
|
1.0
|
N
|
D:GLU10
|
4.6
|
34.3
|
1.0
|
N
|
D:SER61
|
4.6
|
35.8
|
1.0
|
O
|
D:SER59
|
4.7
|
36.4
|
1.0
|
CD2
|
D:HIS60
|
4.7
|
34.0
|
1.0
|
OE1
|
D:GLU133
|
4.8
|
35.7
|
1.0
|
C
|
D:HIS60
|
4.9
|
34.5
|
1.0
|
CA
|
D:ASP8
|
4.9
|
36.8
|
1.0
|
CB
|
D:GLU10
|
5.0
|
33.6
|
1.0
|
|
Zinc binding site 9 out
of 10 in 1hi9
Go back to
Zinc Binding Sites List in 1hi9
Zinc binding site 9 out
of 10 in the Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 9 of Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn300
b:28.9
occ:1.00
|
OE1
|
E:GLU133
|
1.9
|
32.6
|
1.0
|
NE2
|
E:HIS104
|
2.0
|
26.6
|
1.0
|
O
|
E:HOH2073
|
2.0
|
24.0
|
1.0
|
OD2
|
E:ASP8
|
2.1
|
29.8
|
1.0
|
CD
|
E:GLU133
|
2.5
|
33.7
|
1.0
|
OE2
|
E:GLU133
|
2.6
|
31.6
|
1.0
|
CE1
|
E:HIS104
|
2.9
|
30.4
|
1.0
|
CD2
|
E:HIS104
|
3.0
|
30.7
|
1.0
|
CG
|
E:ASP8
|
3.1
|
33.4
|
1.0
|
ZN
|
E:ZN301
|
3.2
|
51.3
|
1.0
|
NE2
|
E:HIS115
|
3.6
|
38.9
|
1.0
|
OD1
|
E:ASP8
|
3.6
|
31.6
|
1.0
|
OE1
|
E:GLU10
|
3.9
|
35.2
|
1.0
|
CE1
|
E:HIS115
|
3.9
|
38.8
|
1.0
|
CG
|
E:GLU133
|
4.0
|
35.0
|
1.0
|
ND1
|
E:HIS104
|
4.0
|
28.4
|
1.0
|
CG
|
E:HIS104
|
4.1
|
31.1
|
1.0
|
CE
|
E:MET87
|
4.1
|
33.1
|
1.0
|
CB
|
E:ASP8
|
4.4
|
34.0
|
1.0
|
CD2
|
E:HIS115
|
4.5
|
36.9
|
1.0
|
CD
|
E:GLU10
|
4.6
|
33.9
|
1.0
|
CB
|
E:GLU133
|
4.6
|
34.5
|
1.0
|
SD
|
E:MET87
|
4.8
|
30.2
|
1.0
|
OE2
|
E:GLU10
|
4.9
|
34.4
|
1.0
|
ND1
|
E:HIS115
|
5.0
|
36.1
|
1.0
|
|
Zinc binding site 10 out
of 10 in 1hi9
Go back to
Zinc Binding Sites List in 1hi9
Zinc binding site 10 out
of 10 in the Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 10 of Zn-Dependent D-Aminopeptidase Dppa From Bacillus Subtilis, A Self- Compartmentalizing Protease. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn301
b:51.3
occ:1.00
|
OE1
|
E:GLU10
|
2.3
|
35.2
|
1.0
|
OD1
|
E:ASP8
|
2.3
|
31.6
|
1.0
|
ND1
|
E:HIS60
|
2.5
|
30.8
|
1.0
|
O
|
E:HOH2073
|
2.5
|
24.0
|
1.0
|
OE2
|
E:GLU10
|
2.8
|
34.4
|
1.0
|
CD
|
E:GLU10
|
2.9
|
33.9
|
1.0
|
CG
|
E:ASP8
|
3.1
|
33.4
|
1.0
|
OD2
|
E:ASP8
|
3.2
|
29.8
|
1.0
|
ZN
|
E:ZN300
|
3.2
|
28.9
|
1.0
|
CE1
|
E:HIS60
|
3.3
|
32.0
|
1.0
|
CG
|
E:HIS60
|
3.6
|
31.6
|
1.0
|
CB
|
E:HIS60
|
3.9
|
33.3
|
1.0
|
CA
|
E:HIS60
|
4.1
|
34.2
|
1.0
|
NE2
|
E:HIS115
|
4.2
|
38.9
|
1.0
|
N
|
E:MET9
|
4.2
|
33.4
|
1.0
|
NE2
|
E:HIS104
|
4.2
|
26.6
|
1.0
|
CG
|
E:GLU10
|
4.4
|
35.3
|
1.0
|
CE1
|
E:HIS115
|
4.4
|
38.8
|
1.0
|
CB
|
E:ASP8
|
4.4
|
34.0
|
1.0
|
CD2
|
E:HIS104
|
4.5
|
30.7
|
1.0
|
NE2
|
E:HIS60
|
4.5
|
32.2
|
1.0
|
N
|
E:GLU10
|
4.6
|
33.5
|
1.0
|
O
|
E:HOH2002
|
4.6
|
38.0
|
1.0
|
N
|
E:SER61
|
4.6
|
35.8
|
1.0
|
CD2
|
E:HIS60
|
4.6
|
31.9
|
1.0
|
O
|
E:SER59
|
4.6
|
30.3
|
1.0
|
OE1
|
E:GLU133
|
4.8
|
32.6
|
1.0
|
C
|
E:HIS60
|
4.9
|
35.1
|
1.0
|
CA
|
E:ASP8
|
4.9
|
33.6
|
1.0
|
CB
|
E:MET9
|
4.9
|
35.2
|
1.0
|
CB
|
E:GLU10
|
5.0
|
33.0
|
1.0
|
CA
|
E:MET9
|
5.0
|
35.1
|
1.0
|
|
Reference:
H.Remaut,
C.Bompard-Gilles,
C.Goffin,
J.M.Frere,
J.Van Beeumen.
Structure of the Bacillus Subtilis D-Aminopeptidase Dppa Reveals A Novel Self-Compartmentalizing Protease Nat.Struct.Biol. V. 8 674 2001.
ISSN: ISSN 1072-8368
PubMed: 11473256
DOI: 10.1038/90380
Page generated: Sun Oct 13 02:15:08 2024
|