Manganese in PDB 1m35: Aminopeptidase P From Escherichia Coli
Enzymatic activity of Aminopeptidase P From Escherichia Coli
All present enzymatic activity of Aminopeptidase P From Escherichia Coli:
3.4.11.9;
Protein crystallography data
The structure of Aminopeptidase P From Escherichia Coli, PDB code: 1m35
was solved by
S.C.Graham,
M.Lee,
H.C.Freeman,
J.M.Guss,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
19.99 /
2.40
|
|
Space group
|
C 2 2 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
209.047,
313.963,
162.034,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
19.5 /
21.5
|
Manganese Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Manganese atom in the Aminopeptidase P From Escherichia Coli
(pdb code 1m35). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 12 binding sites of Manganese where determined in the
Aminopeptidase P From Escherichia Coli, PDB code: 1m35:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Manganese binding site 1 out
of 12 in 1m35
Go back to
Manganese Binding Sites List in 1m35
Manganese binding site 1 out
of 12 in the Aminopeptidase P From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Aminopeptidase P From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn2001
b:25.4
occ:1.00
|
OD1
|
A:ASP271
|
2.0
|
19.0
|
1.0
|
|
O
|
A:HOH2150
|
2.1
|
19.6
|
1.0
|
|
OE1
|
A:GLU406
|
2.2
|
23.2
|
1.0
|
|
OD2
|
A:ASP260
|
2.3
|
19.8
|
1.0
|
|
OD1
|
A:ASP260
|
2.3
|
19.8
|
1.0
|
|
O
|
A:HOH2042
|
2.4
|
24.1
|
1.0
|
|
CG
|
A:ASP260
|
2.6
|
19.8
|
1.0
|
|
CG
|
A:ASP271
|
2.9
|
19.0
|
1.0
|
|
CD
|
A:GLU406
|
3.1
|
23.2
|
1.0
|
|
MN
|
A:MN2002
|
3.2
|
22.5
|
1.0
|
|
OD2
|
A:ASP271
|
3.2
|
19.0
|
1.0
|
|
OE2
|
A:GLU406
|
3.3
|
23.2
|
1.0
|
|
OG1
|
A:THR273
|
3.6
|
22.9
|
1.0
|
|
OH
|
A:TYR229
|
3.7
|
31.4
|
1.0
|
|
O
|
A:HOH2209
|
3.9
|
36.5
|
1.0
|
|
OE1
|
A:GLU383
|
4.0
|
32.6
|
1.0
|
|
CB
|
A:ASP260
|
4.1
|
19.8
|
1.0
|
|
CZ
|
A:TYR229
|
4.2
|
31.4
|
1.0
|
|
CB
|
A:ASP271
|
4.4
|
19.0
|
1.0
|
|
CE2
|
A:TYR229
|
4.5
|
31.4
|
1.0
|
|
CG
|
A:GLU406
|
4.5
|
19.1
|
1.0
|
|
C
|
A:ASP271
|
4.6
|
28.4
|
1.0
|
|
CD
|
A:GLU383
|
4.7
|
32.6
|
1.0
|
|
O
|
A:ILE272
|
4.7
|
24.2
|
1.0
|
|
OE2
|
A:GLU383
|
4.7
|
32.6
|
1.0
|
|
CA
|
A:ASP271
|
4.8
|
28.4
|
1.0
|
|
N
|
A:ILE272
|
4.8
|
24.2
|
1.0
|
|
O
|
A:ASP271
|
4.8
|
28.4
|
1.0
|
|
C
|
A:ILE272
|
4.8
|
24.2
|
1.0
|
|
NE
|
A:ARG404
|
4.9
|
24.2
|
1.0
|
|
CA
|
A:ASP260
|
4.9
|
26.6
|
1.0
|
|
CE1
|
A:TYR229
|
4.9
|
31.4
|
1.0
|
|
CB
|
A:THR273
|
5.0
|
22.9
|
1.0
|
|
NH2
|
A:ARG404
|
5.0
|
24.2
|
1.0
|
|
Manganese binding site 2 out
of 12 in 1m35
Go back to
Manganese Binding Sites List in 1m35
Manganese binding site 2 out
of 12 in the Aminopeptidase P From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Aminopeptidase P From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn2002
b:22.5
occ:1.00
|
OD2
|
A:ASP271
|
2.0
|
19.0
|
1.0
|
|
O
|
A:HOH2150
|
2.0
|
19.6
|
1.0
|
|
NE2
|
A:HIS354
|
2.1
|
20.9
|
1.0
|
|
OE2
|
A:GLU406
|
2.1
|
23.2
|
1.0
|
|
OE2
|
A:GLU383
|
2.2
|
32.6
|
1.0
|
|
CG
|
A:ASP271
|
3.0
|
19.0
|
1.0
|
|
CD
|
A:GLU383
|
3.0
|
32.6
|
1.0
|
|
CD2
|
A:HIS354
|
3.1
|
20.9
|
1.0
|
|
OE1
|
A:GLU383
|
3.1
|
32.6
|
1.0
|
|
CD
|
A:GLU406
|
3.1
|
23.2
|
1.0
|
|
CE1
|
A:HIS354
|
3.1
|
20.9
|
1.0
|
|
MN
|
A:MN2001
|
3.2
|
25.4
|
1.0
|
|
OD1
|
A:ASP271
|
3.3
|
19.0
|
1.0
|
|
O
|
A:HOH2209
|
3.4
|
36.5
|
1.0
|
|
OE1
|
A:GLU406
|
3.4
|
23.2
|
1.0
|
|
OG1
|
A:THR381
|
3.9
|
26.4
|
1.0
|
|
CG2
|
A:THR381
|
3.9
|
26.4
|
1.0
|
|
O
|
A:HOH2042
|
3.9
|
24.1
|
1.0
|
|
CB
|
A:THR381
|
4.2
|
26.4
|
1.0
|
|
CG
|
A:HIS354
|
4.2
|
20.9
|
1.0
|
|
ND1
|
A:HIS354
|
4.2
|
20.9
|
1.0
|
|
CB
|
A:ASP271
|
4.3
|
19.0
|
1.0
|
|
CG
|
A:GLU383
|
4.4
|
30.1
|
1.0
|
|
CG
|
A:GLU406
|
4.5
|
19.1
|
1.0
|
|
NE2
|
A:HIS361
|
4.7
|
34.7
|
1.0
|
|
CG2
|
A:VAL360
|
4.9
|
18.3
|
1.0
|
|
CD2
|
A:HIS361
|
4.9
|
34.7
|
1.0
|
|
Manganese binding site 3 out
of 12 in 1m35
Go back to
Manganese Binding Sites List in 1m35
Manganese binding site 3 out
of 12 in the Aminopeptidase P From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Aminopeptidase P From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn2003
b:25.3
occ:1.00
|
O
|
B:HOH2202
|
2.0
|
23.6
|
1.0
|
|
OD1
|
B:ASP271
|
2.0
|
19.9
|
1.0
|
|
OE1
|
B:GLU406
|
2.1
|
29.5
|
1.0
|
|
OD2
|
B:ASP260
|
2.3
|
24.1
|
1.0
|
|
OD1
|
B:ASP260
|
2.3
|
24.1
|
1.0
|
|
O
|
B:HOH2203
|
2.5
|
26.4
|
1.0
|
|
CG
|
B:ASP260
|
2.6
|
24.1
|
1.0
|
|
CG
|
B:ASP271
|
2.9
|
19.9
|
1.0
|
|
CD
|
B:GLU406
|
3.1
|
29.5
|
1.0
|
|
OD2
|
B:ASP271
|
3.2
|
19.9
|
1.0
|
|
MN
|
B:MN2004
|
3.2
|
23.4
|
1.0
|
|
OE2
|
B:GLU406
|
3.3
|
29.5
|
1.0
|
|
OG1
|
B:THR273
|
3.5
|
28.6
|
1.0
|
|
OH
|
B:TYR229
|
3.7
|
26.8
|
1.0
|
|
O
|
B:HOH2235
|
3.8
|
38.8
|
1.0
|
|
OE1
|
B:GLU383
|
4.0
|
34.4
|
1.0
|
|
CB
|
B:ASP260
|
4.1
|
24.1
|
1.0
|
|
CZ
|
B:TYR229
|
4.2
|
26.8
|
1.0
|
|
CB
|
B:ASP271
|
4.4
|
19.9
|
1.0
|
|
CG
|
B:GLU406
|
4.5
|
26.3
|
1.0
|
|
CE2
|
B:TYR229
|
4.5
|
26.8
|
1.0
|
|
C
|
B:ASP271
|
4.6
|
24.9
|
1.0
|
|
O
|
B:ILE272
|
4.7
|
26.6
|
1.0
|
|
CD
|
B:GLU383
|
4.7
|
34.4
|
1.0
|
|
OE2
|
B:GLU383
|
4.7
|
34.4
|
1.0
|
|
CA
|
B:ASP271
|
4.7
|
24.9
|
1.0
|
|
N
|
B:ILE272
|
4.8
|
26.6
|
1.0
|
|
O
|
B:ASP271
|
4.8
|
24.9
|
1.0
|
|
C
|
B:ILE272
|
4.8
|
26.6
|
1.0
|
|
CA
|
B:ASP260
|
4.9
|
25.9
|
1.0
|
|
NE
|
B:ARG404
|
4.9
|
27.0
|
1.0
|
|
CB
|
B:THR273
|
4.9
|
28.6
|
1.0
|
|
NH2
|
B:ARG404
|
5.0
|
27.0
|
1.0
|
|
CE1
|
B:TYR229
|
5.0
|
26.8
|
1.0
|
|
Manganese binding site 4 out
of 12 in 1m35
Go back to
Manganese Binding Sites List in 1m35
Manganese binding site 4 out
of 12 in the Aminopeptidase P From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Aminopeptidase P From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn2004
b:23.4
occ:1.00
|
OD2
|
B:ASP271
|
1.9
|
19.9
|
1.0
|
|
O
|
B:HOH2202
|
2.0
|
23.6
|
1.0
|
|
OE2
|
B:GLU406
|
2.1
|
29.5
|
1.0
|
|
NE2
|
B:HIS354
|
2.1
|
20.4
|
1.0
|
|
OE2
|
B:GLU383
|
2.2
|
34.4
|
1.0
|
|
CG
|
B:ASP271
|
2.9
|
19.9
|
1.0
|
|
CD
|
B:GLU383
|
3.0
|
34.4
|
1.0
|
|
CD2
|
B:HIS354
|
3.1
|
20.4
|
1.0
|
|
CE1
|
B:HIS354
|
3.1
|
20.4
|
1.0
|
|
CD
|
B:GLU406
|
3.1
|
29.5
|
1.0
|
|
OE1
|
B:GLU383
|
3.2
|
34.4
|
1.0
|
|
MN
|
B:MN2003
|
3.2
|
25.3
|
1.0
|
|
O
|
B:HOH2235
|
3.3
|
38.8
|
1.0
|
|
OD1
|
B:ASP271
|
3.4
|
19.9
|
1.0
|
|
OE1
|
B:GLU406
|
3.5
|
29.5
|
1.0
|
|
OG1
|
B:THR381
|
3.8
|
30.1
|
1.0
|
|
CG2
|
B:THR381
|
3.8
|
30.1
|
1.0
|
|
O
|
B:HOH2203
|
4.0
|
26.4
|
1.0
|
|
CB
|
B:THR381
|
4.1
|
30.1
|
1.0
|
|
ND1
|
B:HIS354
|
4.2
|
20.4
|
1.0
|
|
CG
|
B:HIS354
|
4.2
|
20.4
|
1.0
|
|
CB
|
B:ASP271
|
4.2
|
19.9
|
1.0
|
|
CG
|
B:GLU383
|
4.4
|
31.4
|
1.0
|
|
CG
|
B:GLU406
|
4.4
|
26.3
|
1.0
|
|
NE2
|
B:HIS361
|
4.8
|
35.2
|
1.0
|
|
CG2
|
B:VAL360
|
4.9
|
20.7
|
1.0
|
|
CD2
|
B:HIS361
|
5.0
|
35.2
|
1.0
|
|
Manganese binding site 5 out
of 12 in 1m35
Go back to
Manganese Binding Sites List in 1m35
Manganese binding site 5 out
of 12 in the Aminopeptidase P From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Aminopeptidase P From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn2005
b:22.3
occ:1.00
|
OD1
|
C:ASP271
|
2.0
|
16.7
|
1.0
|
|
O
|
C:HOH2171
|
2.1
|
20.5
|
1.0
|
|
OE1
|
C:GLU406
|
2.2
|
28.4
|
1.0
|
|
OD2
|
C:ASP260
|
2.2
|
19.8
|
1.0
|
|
OD1
|
C:ASP260
|
2.3
|
19.8
|
1.0
|
|
O
|
C:HOH2049
|
2.5
|
35.5
|
1.0
|
|
CG
|
C:ASP260
|
2.6
|
19.8
|
1.0
|
|
CG
|
C:ASP271
|
3.0
|
16.7
|
1.0
|
|
CD
|
C:GLU406
|
3.1
|
28.4
|
1.0
|
|
MN
|
C:MN2006
|
3.2
|
20.5
|
1.0
|
|
OD2
|
C:ASP271
|
3.2
|
16.7
|
1.0
|
|
OE2
|
C:GLU406
|
3.3
|
28.4
|
1.0
|
|
OG1
|
C:THR273
|
3.5
|
27.0
|
1.0
|
|
OH
|
C:TYR229
|
3.7
|
33.5
|
1.0
|
|
O
|
C:HOH2178
|
4.0
|
43.8
|
1.0
|
|
OE1
|
C:GLU383
|
4.0
|
36.4
|
1.0
|
|
CB
|
C:ASP260
|
4.1
|
19.8
|
1.0
|
|
CZ
|
C:TYR229
|
4.2
|
33.5
|
1.0
|
|
CB
|
C:ASP271
|
4.4
|
16.7
|
1.0
|
|
CE2
|
C:TYR229
|
4.4
|
33.5
|
1.0
|
|
CG
|
C:GLU406
|
4.5
|
30.6
|
1.0
|
|
C
|
C:ASP271
|
4.6
|
28.3
|
1.0
|
|
O
|
C:ILE272
|
4.7
|
26.8
|
1.0
|
|
CD
|
C:GLU383
|
4.7
|
36.4
|
1.0
|
|
OE2
|
C:GLU383
|
4.7
|
36.4
|
1.0
|
|
O
|
C:ASP271
|
4.7
|
28.3
|
1.0
|
|
CA
|
C:ASP271
|
4.8
|
28.3
|
1.0
|
|
N
|
C:ILE272
|
4.8
|
26.8
|
1.0
|
|
C
|
C:ILE272
|
4.8
|
26.8
|
1.0
|
|
CA
|
C:ASP260
|
4.9
|
25.3
|
1.0
|
|
NE
|
C:ARG404
|
4.9
|
23.6
|
1.0
|
|
CB
|
C:THR273
|
4.9
|
27.0
|
1.0
|
|
NH2
|
C:ARG404
|
4.9
|
23.6
|
1.0
|
|
CE1
|
C:TYR229
|
5.0
|
33.5
|
1.0
|
|
Manganese binding site 6 out
of 12 in 1m35
Go back to
Manganese Binding Sites List in 1m35
Manganese binding site 6 out
of 12 in the Aminopeptidase P From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Aminopeptidase P From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn2006
b:20.5
occ:1.00
|
OD2
|
C:ASP271
|
2.0
|
16.7
|
1.0
|
|
OE2
|
C:GLU406
|
2.1
|
28.4
|
1.0
|
|
NE2
|
C:HIS354
|
2.2
|
19.2
|
1.0
|
|
O
|
C:HOH2171
|
2.2
|
20.5
|
1.0
|
|
OE2
|
C:GLU383
|
2.2
|
36.4
|
1.0
|
|
CG
|
C:ASP271
|
3.0
|
16.7
|
1.0
|
|
CD
|
C:GLU383
|
3.0
|
36.4
|
1.0
|
|
CD2
|
C:HIS354
|
3.1
|
19.2
|
1.0
|
|
CD
|
C:GLU406
|
3.1
|
28.4
|
1.0
|
|
OE1
|
C:GLU383
|
3.1
|
36.4
|
1.0
|
|
MN
|
C:MN2005
|
3.2
|
22.3
|
1.0
|
|
CE1
|
C:HIS354
|
3.2
|
19.2
|
1.0
|
|
OD1
|
C:ASP271
|
3.4
|
16.7
|
1.0
|
|
OE1
|
C:GLU406
|
3.4
|
28.4
|
1.0
|
|
O
|
C:HOH2178
|
3.5
|
43.8
|
1.0
|
|
O
|
C:HOH2049
|
3.8
|
35.5
|
1.0
|
|
OG1
|
C:THR381
|
3.9
|
20.6
|
1.0
|
|
CG2
|
C:THR381
|
3.9
|
20.6
|
1.0
|
|
CB
|
C:THR381
|
4.2
|
20.6
|
1.0
|
|
CB
|
C:ASP271
|
4.3
|
16.7
|
1.0
|
|
CG
|
C:HIS354
|
4.3
|
19.2
|
1.0
|
|
ND1
|
C:HIS354
|
4.3
|
19.2
|
1.0
|
|
CG
|
C:GLU383
|
4.4
|
33.5
|
1.0
|
|
CG
|
C:GLU406
|
4.5
|
30.6
|
1.0
|
|
NE2
|
C:HIS361
|
4.7
|
36.5
|
1.0
|
|
CG2
|
C:VAL360
|
4.9
|
26.1
|
1.0
|
|
CD2
|
C:HIS361
|
5.0
|
36.5
|
1.0
|
|
OD2
|
C:ASP260
|
5.0
|
19.8
|
1.0
|
|
Manganese binding site 7 out
of 12 in 1m35
Go back to
Manganese Binding Sites List in 1m35
Manganese binding site 7 out
of 12 in the Aminopeptidase P From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 7 of Aminopeptidase P From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn2007
b:23.8
occ:1.00
|
OD1
|
D:ASP271
|
2.0
|
18.3
|
1.0
|
|
O
|
D:HOH2226
|
2.0
|
26.7
|
1.0
|
|
OE1
|
D:GLU406
|
2.1
|
31.8
|
1.0
|
|
OD2
|
D:ASP260
|
2.3
|
19.8
|
1.0
|
|
OD1
|
D:ASP260
|
2.3
|
19.8
|
1.0
|
|
CG
|
D:ASP260
|
2.6
|
19.8
|
1.0
|
|
O
|
D:HOH2067
|
2.7
|
35.3
|
1.0
|
|
CG
|
D:ASP271
|
2.9
|
18.3
|
1.0
|
|
CD
|
D:GLU406
|
3.0
|
31.8
|
1.0
|
|
MN
|
D:MN2008
|
3.1
|
23.2
|
1.0
|
|
OD2
|
D:ASP271
|
3.1
|
18.3
|
1.0
|
|
OE2
|
D:GLU406
|
3.3
|
31.8
|
1.0
|
|
OG1
|
D:THR273
|
3.5
|
28.9
|
1.0
|
|
OH
|
D:TYR229
|
3.7
|
29.9
|
1.0
|
|
O
|
D:HOH2274
|
3.9
|
41.4
|
1.0
|
|
OE1
|
D:GLU383
|
4.0
|
41.7
|
1.0
|
|
CB
|
D:ASP260
|
4.1
|
19.8
|
1.0
|
|
CZ
|
D:TYR229
|
4.2
|
29.9
|
1.0
|
|
CB
|
D:ASP271
|
4.3
|
18.3
|
1.0
|
|
CG
|
D:GLU406
|
4.4
|
27.2
|
1.0
|
|
CE2
|
D:TYR229
|
4.5
|
29.9
|
1.0
|
|
C
|
D:ASP271
|
4.5
|
29.9
|
1.0
|
|
CD
|
D:GLU383
|
4.6
|
41.7
|
1.0
|
|
O
|
D:ILE272
|
4.7
|
26.0
|
1.0
|
|
OE2
|
D:GLU383
|
4.7
|
41.7
|
1.0
|
|
CA
|
D:ASP271
|
4.7
|
29.9
|
1.0
|
|
O
|
D:ASP271
|
4.7
|
29.9
|
1.0
|
|
N
|
D:ILE272
|
4.8
|
26.0
|
1.0
|
|
C
|
D:ILE272
|
4.8
|
26.0
|
1.0
|
|
NE
|
D:ARG404
|
4.9
|
25.8
|
1.0
|
|
CB
|
D:THR273
|
4.9
|
28.9
|
1.0
|
|
CA
|
D:ASP260
|
4.9
|
24.5
|
1.0
|
|
NH2
|
D:ARG404
|
5.0
|
25.8
|
1.0
|
|
CE1
|
D:TYR229
|
5.0
|
29.9
|
1.0
|
|
Manganese binding site 8 out
of 12 in 1m35
Go back to
Manganese Binding Sites List in 1m35
Manganese binding site 8 out
of 12 in the Aminopeptidase P From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 8 of Aminopeptidase P From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn2008
b:23.2
occ:1.00
|
OD2
|
D:ASP271
|
1.9
|
18.3
|
1.0
|
|
O
|
D:HOH2226
|
2.0
|
26.7
|
1.0
|
|
OE2
|
D:GLU406
|
2.1
|
31.8
|
1.0
|
|
NE2
|
D:HIS354
|
2.1
|
21.6
|
1.0
|
|
OE2
|
D:GLU383
|
2.2
|
41.7
|
1.0
|
|
CG
|
D:ASP271
|
2.9
|
18.3
|
1.0
|
|
CD
|
D:GLU383
|
3.0
|
41.7
|
1.0
|
|
CD2
|
D:HIS354
|
3.1
|
21.6
|
1.0
|
|
CE1
|
D:HIS354
|
3.1
|
21.6
|
1.0
|
|
CD
|
D:GLU406
|
3.1
|
31.8
|
1.0
|
|
MN
|
D:MN2007
|
3.1
|
23.8
|
1.0
|
|
O
|
D:HOH2274
|
3.1
|
41.4
|
1.0
|
|
OE1
|
D:GLU383
|
3.2
|
41.7
|
1.0
|
|
OD1
|
D:ASP271
|
3.4
|
18.3
|
1.0
|
|
OE1
|
D:GLU406
|
3.4
|
31.8
|
1.0
|
|
OG1
|
D:THR381
|
3.8
|
26.0
|
1.0
|
|
O
|
D:HOH2067
|
3.9
|
35.3
|
1.0
|
|
CG2
|
D:THR381
|
3.9
|
26.0
|
1.0
|
|
CB
|
D:THR381
|
4.1
|
26.0
|
1.0
|
|
ND1
|
D:HIS354
|
4.2
|
21.6
|
1.0
|
|
CB
|
D:ASP271
|
4.2
|
18.3
|
1.0
|
|
CG
|
D:HIS354
|
4.2
|
21.6
|
1.0
|
|
CG
|
D:GLU383
|
4.4
|
31.2
|
1.0
|
|
CG
|
D:GLU406
|
4.5
|
27.2
|
1.0
|
|
NE2
|
D:HIS361
|
4.7
|
36.8
|
1.0
|
|
CG2
|
D:VAL360
|
4.9
|
20.4
|
1.0
|
|
CD2
|
D:HIS361
|
5.0
|
36.8
|
1.0
|
|
Manganese binding site 9 out
of 12 in 1m35
Go back to
Manganese Binding Sites List in 1m35
Manganese binding site 9 out
of 12 in the Aminopeptidase P From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 9 of Aminopeptidase P From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn2009
b:22.3
occ:1.00
|
O
|
E:HOH1309
|
1.9
|
15.1
|
1.0
|
|
OD1
|
E:ASP271
|
2.1
|
25.0
|
1.0
|
|
OE1
|
E:GLU406
|
2.1
|
22.2
|
1.0
|
|
OD1
|
E:ASP260
|
2.2
|
21.9
|
1.0
|
|
OD2
|
E:ASP260
|
2.2
|
21.9
|
1.0
|
|
O
|
E:HOH614
|
2.3
|
23.7
|
1.0
|
|
CG
|
E:ASP260
|
2.5
|
21.9
|
1.0
|
|
CG
|
E:ASP271
|
3.0
|
25.0
|
1.0
|
|
CD
|
E:GLU406
|
3.1
|
22.2
|
1.0
|
|
OD2
|
E:ASP271
|
3.2
|
25.0
|
1.0
|
|
MN
|
E:MN2010
|
3.3
|
20.0
|
1.0
|
|
OE2
|
E:GLU406
|
3.4
|
22.2
|
1.0
|
|
OG1
|
E:THR273
|
3.5
|
25.5
|
1.0
|
|
O
|
E:HOH1610
|
3.6
|
54.9
|
1.0
|
|
OH
|
E:TYR229
|
3.7
|
29.2
|
1.0
|
|
OE1
|
E:GLU383
|
4.0
|
29.5
|
1.0
|
|
CB
|
E:ASP260
|
4.1
|
21.9
|
1.0
|
|
CZ
|
E:TYR229
|
4.1
|
29.2
|
1.0
|
|
CB
|
E:ASP271
|
4.4
|
25.0
|
1.0
|
|
CE2
|
E:TYR229
|
4.4
|
29.2
|
1.0
|
|
CG
|
E:GLU406
|
4.5
|
16.2
|
1.0
|
|
C
|
E:ASP271
|
4.6
|
23.0
|
1.0
|
|
O
|
E:ILE272
|
4.6
|
22.1
|
1.0
|
|
CD
|
E:GLU383
|
4.7
|
29.5
|
1.0
|
|
N
|
E:ILE272
|
4.7
|
22.1
|
1.0
|
|
OE2
|
E:GLU383
|
4.8
|
29.5
|
1.0
|
|
CA
|
E:ASP271
|
4.8
|
23.0
|
1.0
|
|
C
|
E:ILE272
|
4.8
|
22.1
|
1.0
|
|
O
|
E:ASP271
|
4.8
|
23.0
|
1.0
|
|
CA
|
E:ASP260
|
4.8
|
23.3
|
1.0
|
|
NE
|
E:ARG404
|
4.8
|
23.9
|
1.0
|
|
CB
|
E:THR273
|
4.9
|
25.5
|
1.0
|
|
NH2
|
E:ARG404
|
4.9
|
23.9
|
1.0
|
|
CE1
|
E:TYR229
|
4.9
|
29.2
|
1.0
|
|
Manganese binding site 10 out
of 12 in 1m35
Go back to
Manganese Binding Sites List in 1m35
Manganese binding site 10 out
of 12 in the Aminopeptidase P From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 10 of Aminopeptidase P From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn2010
b:20.0
occ:1.00
|
OD2
|
E:ASP271
|
1.9
|
25.0
|
1.0
|
|
O
|
E:HOH1309
|
2.0
|
15.1
|
1.0
|
|
OE2
|
E:GLU406
|
2.0
|
22.2
|
1.0
|
|
NE2
|
E:HIS354
|
2.1
|
19.9
|
1.0
|
|
OE2
|
E:GLU383
|
2.2
|
29.5
|
1.0
|
|
CG
|
E:ASP271
|
3.0
|
25.0
|
1.0
|
|
CD
|
E:GLU383
|
3.0
|
29.5
|
1.0
|
|
O
|
E:HOH1610
|
3.0
|
54.9
|
1.0
|
|
CD2
|
E:HIS354
|
3.0
|
19.9
|
1.0
|
|
CD
|
E:GLU406
|
3.1
|
22.2
|
1.0
|
|
CE1
|
E:HIS354
|
3.1
|
19.9
|
1.0
|
|
OE1
|
E:GLU383
|
3.1
|
29.5
|
1.0
|
|
MN
|
E:MN2009
|
3.3
|
22.3
|
1.0
|
|
OE1
|
E:GLU406
|
3.4
|
22.2
|
1.0
|
|
OD1
|
E:ASP271
|
3.4
|
25.0
|
1.0
|
|
OG1
|
E:THR381
|
3.8
|
22.6
|
1.0
|
|
CG2
|
E:THR381
|
3.8
|
22.6
|
1.0
|
|
O
|
E:HOH614
|
3.9
|
23.7
|
1.0
|
|
CB
|
E:THR381
|
4.1
|
22.6
|
1.0
|
|
CG
|
E:HIS354
|
4.2
|
19.9
|
1.0
|
|
ND1
|
E:HIS354
|
4.2
|
19.9
|
1.0
|
|
CB
|
E:ASP271
|
4.2
|
25.0
|
1.0
|
|
CG
|
E:GLU383
|
4.4
|
18.1
|
1.0
|
|
CG
|
E:GLU406
|
4.4
|
16.2
|
1.0
|
|
NE2
|
E:HIS361
|
4.7
|
32.0
|
1.0
|
|
CG2
|
E:VAL360
|
4.9
|
20.1
|
1.0
|
|
CD2
|
E:HIS361
|
5.0
|
32.0
|
1.0
|
|
Reference:
S.C.Graham,
M.Lee,
H.C.Freeman,
J.M.Guss.
An Orthorhombic Form of Escherichia Coli Aminopeptidase P at 2.4 A Resolution. Acta Crystallogr.,Sect.D V. 59 897 2003.
ISSN: ISSN 0907-4449
PubMed: 12777807
DOI: 10.1107/S0907444903005870
Page generated: Sat Oct 5 11:38:39 2024
|
