Chlorine in PDB 1rtm: Trimeric Structure of A C-Type Mannose-Binding Protein
Protein crystallography data
The structure of Trimeric Structure of A C-Type Mannose-Binding Protein, PDB code: 1rtm
was solved by
W.I.Weis,
K.Drickamer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
10.00 /
1.80
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
80.000,
85.100,
98.500,
90.00,
106.30,
90.00
|
R / Rfree (%)
|
22 /
27
|
Other elements in 1rtm:
The structure of Trimeric Structure of A C-Type Mannose-Binding Protein also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Trimeric Structure of A C-Type Mannose-Binding Protein
(pdb code 1rtm). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the
Trimeric Structure of A C-Type Mannose-Binding Protein, PDB code: 1rtm:
Jump to Chlorine binding site number:
1;
2;
3;
Chlorine binding site 1 out
of 3 in 1rtm
Go back to
Chlorine Binding Sites List in 1rtm
Chlorine binding site 1 out
of 3 in the Trimeric Structure of A C-Type Mannose-Binding Protein
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Trimeric Structure of A C-Type Mannose-Binding Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
1:Cl4
b:21.5
occ:1.00
|
O
|
1:HOH285
|
3.2
|
21.3
|
1.0
|
N
|
1:CYS209
|
3.3
|
21.0
|
1.0
|
N
|
1:ASP194
|
3.3
|
15.6
|
1.0
|
CA
|
1:SER208
|
3.7
|
20.8
|
1.0
|
CB
|
1:ASP194
|
3.8
|
18.3
|
1.0
|
SG
|
1:CYS209
|
3.9
|
20.2
|
1.0
|
CB
|
1:CYS209
|
3.9
|
18.5
|
1.0
|
C
|
1:SER208
|
4.0
|
20.1
|
1.0
|
CA
|
1:ASP194
|
4.0
|
15.8
|
1.0
|
CA
|
1:GLU193
|
4.1
|
20.0
|
1.0
|
C
|
1:GLU193
|
4.1
|
17.8
|
1.0
|
OG
|
1:SER208
|
4.2
|
20.9
|
1.0
|
CA
|
1:CYS209
|
4.2
|
21.3
|
1.0
|
CG
|
1:ASP194
|
4.2
|
18.9
|
1.0
|
NE2
|
1:GLN210
|
4.2
|
38.1
|
1.0
|
O
|
1:GLY192
|
4.3
|
19.7
|
1.0
|
O
|
1:HOH342
|
4.3
|
37.4
|
1.0
|
O
|
1:HOH232
|
4.4
|
27.7
|
1.0
|
O
|
1:ILE207
|
4.4
|
18.6
|
1.0
|
OD2
|
1:ASP194
|
4.4
|
17.1
|
1.0
|
CB
|
1:SER208
|
4.4
|
21.8
|
1.0
|
N
|
1:GLU193
|
4.6
|
20.6
|
1.0
|
N
|
1:CYS195
|
4.6
|
17.1
|
1.0
|
C
|
1:GLY192
|
4.7
|
20.1
|
1.0
|
N
|
1:SER208
|
4.8
|
18.0
|
1.0
|
C
|
1:ASP194
|
4.8
|
16.0
|
1.0
|
OD1
|
1:ASP194
|
4.9
|
16.5
|
1.0
|
C
|
1:ILE207
|
5.0
|
19.9
|
1.0
|
|
Chlorine binding site 2 out
of 3 in 1rtm
Go back to
Chlorine Binding Sites List in 1rtm
Chlorine binding site 2 out
of 3 in the Trimeric Structure of A C-Type Mannose-Binding Protein
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Trimeric Structure of A C-Type Mannose-Binding Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
2:Cl4
b:40.1
occ:1.00
|
N
|
2:ASP194
|
2.8
|
27.6
|
1.0
|
N
|
2:CYS209
|
3.4
|
27.6
|
1.0
|
CA
|
2:SER208
|
3.6
|
27.4
|
1.0
|
CB
|
2:ASP194
|
3.6
|
26.6
|
1.0
|
CA
|
2:ASP194
|
3.7
|
26.6
|
1.0
|
CA
|
2:GLU193
|
3.7
|
30.0
|
1.0
|
C
|
2:GLU193
|
3.7
|
28.7
|
1.0
|
SG
|
2:CYS209
|
3.8
|
29.0
|
1.0
|
C
|
2:SER208
|
4.0
|
27.6
|
1.0
|
O
|
2:GLY192
|
4.1
|
31.5
|
1.0
|
OG
|
2:SER208
|
4.1
|
26.1
|
1.0
|
CG
|
2:ASP194
|
4.2
|
26.1
|
1.0
|
N
|
2:GLU193
|
4.2
|
31.2
|
1.0
|
CB
|
2:CYS209
|
4.2
|
28.6
|
1.0
|
CB
|
2:SER208
|
4.3
|
29.6
|
1.0
|
OE1
|
2:GLN210
|
4.3
|
46.2
|
1.0
|
O
|
2:ILE207
|
4.3
|
26.2
|
1.0
|
C
|
2:GLY192
|
4.3
|
32.2
|
1.0
|
O
|
2:HOH301
|
4.4
|
40.0
|
1.0
|
N
|
2:CYS195
|
4.4
|
23.7
|
1.0
|
C
|
2:ASP194
|
4.4
|
25.5
|
1.0
|
CA
|
2:CYS209
|
4.4
|
28.6
|
1.0
|
OD2
|
2:ASP194
|
4.6
|
27.3
|
1.0
|
N
|
2:SER208
|
4.6
|
27.4
|
1.0
|
OD1
|
2:ASP194
|
4.7
|
24.0
|
1.0
|
C
|
2:ILE207
|
4.9
|
26.4
|
1.0
|
O
|
2:GLU193
|
4.9
|
28.6
|
1.0
|
|
Chlorine binding site 3 out
of 3 in 1rtm
Go back to
Chlorine Binding Sites List in 1rtm
Chlorine binding site 3 out
of 3 in the Trimeric Structure of A C-Type Mannose-Binding Protein
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of Trimeric Structure of A C-Type Mannose-Binding Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
3:Cl4
b:25.0
occ:1.00
|
O
|
3:HOH322
|
2.3
|
65.0
|
1.0
|
O
|
3:HOH235
|
3.1
|
23.2
|
1.0
|
N
|
3:CYS209
|
3.3
|
24.2
|
1.0
|
N
|
3:ASP194
|
3.4
|
22.6
|
1.0
|
OE1
|
3:GLN210
|
3.7
|
39.6
|
1.0
|
CB
|
3:ASP194
|
3.7
|
24.2
|
1.0
|
CA
|
3:SER208
|
3.8
|
25.8
|
1.0
|
SG
|
3:CYS209
|
3.8
|
23.3
|
1.0
|
CB
|
3:CYS209
|
4.0
|
23.7
|
1.0
|
CA
|
3:ASP194
|
4.1
|
24.2
|
1.0
|
C
|
3:SER208
|
4.1
|
24.7
|
1.0
|
O
|
3:HOH299
|
4.1
|
40.4
|
1.0
|
OG
|
3:SER208
|
4.1
|
22.4
|
1.0
|
CA
|
3:GLU193
|
4.2
|
21.0
|
1.0
|
CG
|
3:ASP194
|
4.2
|
24.9
|
1.0
|
O
|
3:GLY192
|
4.2
|
25.7
|
1.0
|
C
|
3:GLU193
|
4.2
|
21.9
|
1.0
|
CA
|
3:CYS209
|
4.3
|
25.0
|
1.0
|
OD2
|
3:ASP194
|
4.4
|
23.3
|
1.0
|
O
|
3:ILE207
|
4.4
|
23.2
|
1.0
|
CB
|
3:SER208
|
4.4
|
23.6
|
1.0
|
C
|
3:GLY192
|
4.5
|
24.6
|
1.0
|
N
|
3:GLU193
|
4.5
|
21.3
|
1.0
|
N
|
3:CYS195
|
4.7
|
25.0
|
1.0
|
OD1
|
3:ASP194
|
4.8
|
21.0
|
1.0
|
N
|
3:SER208
|
4.8
|
24.5
|
1.0
|
C
|
3:ASP194
|
4.8
|
23.2
|
1.0
|
CD
|
3:GLN210
|
4.8
|
37.9
|
1.0
|
O
|
3:HOH338
|
4.8
|
56.3
|
1.0
|
|
Reference:
W.I.Weis,
K.Drickamer.
Trimeric Structure of A C-Type Mannose-Binding Protein. Structure V. 2 1227 1994.
ISSN: ISSN 0969-2126
PubMed: 7704532
DOI: 10.1016/S0969-2126(94)00124-3
Page generated: Sat Jul 20 01:59:22 2024
|