Chlorine in PDB 1w2m: Ca-Substituted Form of E. Coli Aminopeptidase P
Enzymatic activity of Ca-Substituted Form of E. Coli Aminopeptidase P
All present enzymatic activity of Ca-Substituted Form of E. Coli Aminopeptidase P:
3.4.11.9;
Protein crystallography data
The structure of Ca-Substituted Form of E. Coli Aminopeptidase P, PDB code: 1w2m
was solved by
S.C.Graham,
C.S.Bond,
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)
|
182.57 /
2.40
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
208.359,
312.688,
160.198,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.5 /
20
|
Other elements in 1w2m:
The structure of Ca-Substituted Form of E. Coli Aminopeptidase P also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Ca-Substituted Form of E. Coli Aminopeptidase P
(pdb code 1w2m). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the
Ca-Substituted Form of E. Coli Aminopeptidase P, PDB code: 1w2m:
Jump to Chlorine binding site number:
1;
2;
3;
4;
5;
6;
Chlorine binding site 1 out
of 6 in 1w2m
Go back to
Chlorine Binding Sites List in 1w2m
Chlorine binding site 1 out
of 6 in the Ca-Substituted Form of E. Coli Aminopeptidase P
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Ca-Substituted Form of E. Coli Aminopeptidase P within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1443
b:45.5
occ:1.00
|
N
|
A:VAL80
|
3.3
|
29.6
|
1.0
|
N
|
A:SER111
|
3.4
|
25.2
|
1.0
|
N
|
A:PHE110
|
3.6
|
25.4
|
1.0
|
CA
|
A:ARG79
|
3.7
|
27.9
|
1.0
|
CB
|
A:SER111
|
3.8
|
25.7
|
1.0
|
OG
|
A:SER111
|
3.9
|
26.4
|
1.0
|
CG1
|
A:VAL80
|
4.0
|
29.8
|
1.0
|
C
|
A:ARG79
|
4.0
|
28.5
|
1.0
|
CB
|
A:VAL80
|
4.0
|
30.8
|
1.0
|
O
|
A:ASN78
|
4.1
|
24.4
|
1.0
|
CB
|
A:PHE110
|
4.1
|
25.3
|
1.0
|
CB
|
A:ALA109
|
4.2
|
25.7
|
1.0
|
CA
|
A:PHE110
|
4.2
|
25.3
|
1.0
|
CA
|
A:SER111
|
4.2
|
25.6
|
1.0
|
C
|
A:PHE110
|
4.3
|
25.4
|
1.0
|
CA
|
A:VAL80
|
4.3
|
30.8
|
1.0
|
C
|
A:ALA109
|
4.3
|
25.5
|
1.0
|
CB
|
A:ARG79
|
4.4
|
28.2
|
1.0
|
CA
|
A:ALA109
|
4.4
|
25.6
|
1.0
|
N
|
A:ARG79
|
4.6
|
26.4
|
1.0
|
CG
|
A:ARG79
|
4.7
|
30.5
|
1.0
|
C
|
A:ASN78
|
4.7
|
24.8
|
1.0
|
|
Chlorine binding site 2 out
of 6 in 1w2m
Go back to
Chlorine Binding Sites List in 1w2m
Chlorine binding site 2 out
of 6 in the Ca-Substituted Form of E. Coli Aminopeptidase P
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Ca-Substituted Form of E. Coli Aminopeptidase P within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl1442
b:44.3
occ:1.00
|
N
|
B:VAL80
|
3.3
|
29.6
|
1.0
|
N
|
B:SER111
|
3.4
|
25.3
|
1.0
|
OG
|
B:SER111
|
3.4
|
27.0
|
1.0
|
N
|
B:PHE110
|
3.7
|
25.4
|
1.0
|
CA
|
B:ARG79
|
3.7
|
27.8
|
1.0
|
CB
|
B:SER111
|
3.8
|
25.4
|
1.0
|
CG1
|
B:VAL80
|
4.0
|
30.9
|
1.0
|
CB
|
B:VAL80
|
4.0
|
31.0
|
1.0
|
C
|
B:ARG79
|
4.0
|
28.5
|
1.0
|
CB
|
B:PHE110
|
4.1
|
25.4
|
1.0
|
O
|
B:ASN78
|
4.2
|
24.2
|
1.0
|
CA
|
B:SER111
|
4.2
|
25.7
|
1.0
|
CA
|
B:PHE110
|
4.2
|
25.4
|
1.0
|
C
|
B:PHE110
|
4.3
|
25.4
|
1.0
|
CA
|
B:VAL80
|
4.3
|
30.9
|
1.0
|
CB
|
B:ALA109
|
4.3
|
25.5
|
1.0
|
C
|
B:ALA109
|
4.4
|
25.4
|
1.0
|
CB
|
B:ARG79
|
4.4
|
28.4
|
1.0
|
CA
|
B:ALA109
|
4.5
|
25.6
|
1.0
|
CG
|
B:ARG79
|
4.6
|
30.8
|
1.0
|
N
|
B:ARG79
|
4.7
|
26.3
|
1.0
|
C
|
B:ASN78
|
4.8
|
24.8
|
1.0
|
|
Chlorine binding site 3 out
of 6 in 1w2m
Go back to
Chlorine Binding Sites List in 1w2m
Chlorine binding site 3 out
of 6 in the Ca-Substituted Form of E. Coli Aminopeptidase P
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of Ca-Substituted Form of E. Coli Aminopeptidase P within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cl1442
b:45.6
occ:1.00
|
N
|
C:SER111
|
3.3
|
25.3
|
1.0
|
N
|
C:VAL80
|
3.4
|
29.7
|
1.0
|
N
|
C:PHE110
|
3.6
|
25.6
|
1.0
|
OG
|
C:SER111
|
3.7
|
26.5
|
1.0
|
CB
|
C:SER111
|
3.7
|
25.6
|
1.0
|
CA
|
C:ARG79
|
3.8
|
27.9
|
1.0
|
CG1
|
C:VAL80
|
3.9
|
30.1
|
1.0
|
CB
|
C:PHE110
|
4.0
|
25.5
|
1.0
|
CA
|
C:SER111
|
4.1
|
25.6
|
1.0
|
CB
|
C:VAL80
|
4.1
|
30.9
|
1.0
|
CA
|
C:PHE110
|
4.1
|
25.4
|
1.0
|
C
|
C:ARG79
|
4.1
|
28.5
|
1.0
|
CB
|
C:ALA109
|
4.2
|
25.9
|
1.0
|
C
|
C:PHE110
|
4.2
|
25.4
|
1.0
|
O
|
C:ASN78
|
4.2
|
24.2
|
1.0
|
C
|
C:ALA109
|
4.3
|
25.5
|
1.0
|
CA
|
C:VAL80
|
4.4
|
30.8
|
1.0
|
CA
|
C:ALA109
|
4.5
|
25.7
|
1.0
|
CB
|
C:ARG79
|
4.6
|
28.4
|
1.0
|
N
|
C:ARG79
|
4.7
|
26.3
|
1.0
|
CG
|
C:ARG79
|
4.7
|
30.5
|
1.0
|
C
|
C:ASN78
|
4.8
|
24.8
|
1.0
|
|
Chlorine binding site 4 out
of 6 in 1w2m
Go back to
Chlorine Binding Sites List in 1w2m
Chlorine binding site 4 out
of 6 in the Ca-Substituted Form of E. Coli Aminopeptidase P
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 4 of Ca-Substituted Form of E. Coli Aminopeptidase P within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cl1445
b:42.4
occ:1.00
|
N
|
D:VAL80
|
3.3
|
29.6
|
1.0
|
N
|
D:SER111
|
3.4
|
25.2
|
1.0
|
N
|
D:PHE110
|
3.6
|
25.3
|
1.0
|
CA
|
D:ARG79
|
3.6
|
27.8
|
1.0
|
OG
|
D:SER111
|
3.7
|
26.7
|
1.0
|
CB
|
D:SER111
|
3.8
|
25.8
|
1.0
|
CG1
|
D:VAL80
|
3.9
|
30.2
|
1.0
|
C
|
D:ARG79
|
4.0
|
28.4
|
1.0
|
CB
|
D:VAL80
|
4.0
|
31.0
|
1.0
|
CB
|
D:PHE110
|
4.1
|
25.2
|
1.0
|
O
|
D:ASN78
|
4.2
|
24.0
|
1.0
|
CA
|
D:PHE110
|
4.2
|
25.3
|
1.0
|
CB
|
D:ALA109
|
4.2
|
25.6
|
1.0
|
CA
|
D:SER111
|
4.2
|
25.7
|
1.0
|
C
|
D:PHE110
|
4.3
|
25.3
|
1.0
|
CA
|
D:VAL80
|
4.3
|
30.8
|
1.0
|
C
|
D:ALA109
|
4.4
|
25.5
|
1.0
|
CB
|
D:ARG79
|
4.4
|
28.4
|
1.0
|
CA
|
D:ALA109
|
4.5
|
25.6
|
1.0
|
N
|
D:ARG79
|
4.6
|
26.1
|
1.0
|
CG
|
D:ARG79
|
4.6
|
30.6
|
1.0
|
C
|
D:ASN78
|
4.7
|
24.6
|
1.0
|
|
Chlorine binding site 5 out
of 6 in 1w2m
Go back to
Chlorine Binding Sites List in 1w2m
Chlorine binding site 5 out
of 6 in the Ca-Substituted Form of E. Coli Aminopeptidase P
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 5 of Ca-Substituted Form of E. Coli Aminopeptidase P within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Cl1443
b:35.4
occ:1.00
|
N
|
E:VAL80
|
3.4
|
29.5
|
1.0
|
N
|
E:SER111
|
3.4
|
25.3
|
1.0
|
N
|
E:PHE110
|
3.6
|
25.4
|
1.0
|
CA
|
E:ARG79
|
3.7
|
27.7
|
1.0
|
CB
|
E:SER111
|
3.8
|
25.2
|
1.0
|
OG
|
E:SER111
|
3.9
|
26.2
|
1.0
|
CG1
|
E:VAL80
|
4.0
|
29.8
|
1.0
|
CB
|
E:VAL80
|
4.1
|
30.8
|
1.0
|
C
|
E:ARG79
|
4.1
|
28.4
|
1.0
|
CB
|
E:PHE110
|
4.1
|
25.4
|
1.0
|
O
|
E:ASN78
|
4.1
|
23.9
|
1.0
|
CA
|
E:SER111
|
4.2
|
25.6
|
1.0
|
CA
|
E:PHE110
|
4.2
|
25.3
|
1.0
|
CB
|
E:ALA109
|
4.2
|
25.5
|
1.0
|
C
|
E:PHE110
|
4.2
|
25.4
|
1.0
|
CA
|
E:VAL80
|
4.4
|
30.7
|
1.0
|
C
|
E:ALA109
|
4.4
|
25.5
|
1.0
|
CB
|
E:ARG79
|
4.4
|
28.1
|
1.0
|
CA
|
E:ALA109
|
4.5
|
25.5
|
1.0
|
N
|
E:ARG79
|
4.6
|
26.2
|
1.0
|
CG
|
E:ARG79
|
4.7
|
30.4
|
1.0
|
C
|
E:ASN78
|
4.7
|
24.6
|
1.0
|
|
Chlorine binding site 6 out
of 6 in 1w2m
Go back to
Chlorine Binding Sites List in 1w2m
Chlorine binding site 6 out
of 6 in the Ca-Substituted Form of E. Coli Aminopeptidase P
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 6 of Ca-Substituted Form of E. Coli Aminopeptidase P within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Cl1444
b:40.2
occ:1.00
|
N
|
F:VAL80
|
3.2
|
29.5
|
1.0
|
N
|
F:SER111
|
3.5
|
25.1
|
1.0
|
N
|
F:PHE110
|
3.5
|
25.4
|
1.0
|
CA
|
F:ARG79
|
3.6
|
27.8
|
1.0
|
C
|
F:ARG79
|
3.9
|
28.5
|
1.0
|
CB
|
F:SER111
|
3.9
|
25.7
|
1.0
|
CB
|
F:VAL80
|
3.9
|
30.7
|
1.0
|
CG1
|
F:VAL80
|
3.9
|
30.0
|
1.0
|
O
|
F:ASN78
|
4.0
|
24.0
|
1.0
|
CB
|
F:PHE110
|
4.0
|
25.8
|
1.0
|
OG
|
F:SER111
|
4.0
|
25.8
|
1.0
|
CB
|
F:ALA109
|
4.1
|
25.6
|
1.0
|
CA
|
F:VAL80
|
4.1
|
30.7
|
1.0
|
CA
|
F:PHE110
|
4.1
|
25.4
|
1.0
|
C
|
F:ALA109
|
4.2
|
25.4
|
1.0
|
C
|
F:PHE110
|
4.3
|
25.3
|
1.0
|
CA
|
F:SER111
|
4.3
|
25.6
|
1.0
|
CA
|
F:ALA109
|
4.3
|
25.5
|
1.0
|
CB
|
F:ARG79
|
4.4
|
28.2
|
1.0
|
N
|
F:ARG79
|
4.5
|
26.3
|
1.0
|
C
|
F:ASN78
|
4.6
|
24.6
|
1.0
|
CG
|
F:ARG79
|
4.7
|
30.9
|
1.0
|
|
Reference:
S.C.Graham,
C.S.Bond,
H.C.Freeman,
J.M.Guss.
Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, A Metalloprotease with A Dinuclear Metal Center. Biochemistry V. 44 13820 2005.
ISSN: ISSN 0006-2960
PubMed: 16229471
DOI: 10.1021/BI0512849
Page generated: Sat Jul 20 03:32:20 2024
|