Cadmium in PDB 1vq8: The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui
Protein crystallography data
The structure of The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui, PDB code: 1vq8
was solved by
T.M.Schmeing,
T.A.Steitz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
2.20
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
211.520,
298.480,
574.908,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
22 /
24.7
|
Other elements in 1vq8:
The structure of The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui also contains other interesting chemical elements:
Cadmium Binding Sites:
The binding sites of Cadmium atom in the The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui
(pdb code 1vq8). This binding sites where shown within
5.0 Angstroms radius around Cadmium atom.
In total 5 binding sites of Cadmium where determined in the
The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui, PDB code: 1vq8:
Jump to Cadmium binding site number:
1;
2;
3;
4;
5;
Cadmium binding site 1 out
of 5 in 1vq8
Go back to
Cadmium Binding Sites List in 1vq8
Cadmium binding site 1 out
of 5 in the The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui
Mono view
Stereo pair view
|
A full contact list of Cadmium with other atoms in the Cd binding
site number 1 of The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cd9205
b:0.2
occ:1.00
|
O
|
0:HOH6780
|
2.5
|
83.2
|
1.0
|
ND1
|
O:HIS40
|
3.1
|
33.5
|
1.0
|
CE1
|
O:HIS40
|
3.5
|
33.5
|
1.0
|
CD2
|
O:LEU7
|
3.8
|
47.5
|
1.0
|
O
|
O:HOH3002
|
4.2
|
55.8
|
1.0
|
CD1
|
O:LEU7
|
4.2
|
47.8
|
1.0
|
CG
|
O:HIS40
|
4.3
|
34.3
|
1.0
|
CG
|
O:ARG37
|
4.4
|
46.2
|
1.0
|
O
|
O:HOH6939
|
4.5
|
60.1
|
1.0
|
NH1
|
O:ARG37
|
4.7
|
44.6
|
1.0
|
CG
|
O:LEU7
|
4.7
|
48.3
|
1.0
|
NE2
|
O:HIS40
|
4.7
|
34.8
|
1.0
|
CZ
|
O:ARG37
|
4.9
|
45.5
|
1.0
|
CB
|
O:HIS40
|
4.9
|
37.5
|
1.0
|
OP2
|
0:G656
|
5.0
|
38.6
|
1.0
|
NE
|
O:ARG37
|
5.0
|
45.0
|
1.0
|
|
Cadmium binding site 2 out
of 5 in 1vq8
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Cadmium Binding Sites List in 1vq8
Cadmium binding site 2 out
of 5 in the The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui
Mono view
Stereo pair view
|
A full contact list of Cadmium with other atoms in the Cd binding
site number 2 of The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
U:Cd9201
b:59.0
occ:1.00
|
SG
|
U:CYS36
|
2.4
|
48.2
|
1.0
|
SG
|
U:CYS6
|
2.5
|
45.5
|
1.0
|
SG
|
U:CYS9
|
2.5
|
49.6
|
1.0
|
SG
|
U:CYS32
|
2.6
|
40.2
|
1.0
|
CB
|
U:CYS6
|
3.2
|
45.9
|
1.0
|
CB
|
U:CYS9
|
3.4
|
45.4
|
1.0
|
CB
|
U:CYS36
|
3.6
|
45.5
|
1.0
|
CB
|
U:CYS32
|
3.7
|
40.0
|
1.0
|
N
|
U:CYS9
|
3.8
|
45.2
|
1.0
|
N
|
U:CYS32
|
4.1
|
40.4
|
1.0
|
CA
|
U:CYS9
|
4.2
|
46.6
|
1.0
|
OG1
|
U:THR11
|
4.4
|
52.6
|
1.0
|
CA
|
U:CYS32
|
4.4
|
41.3
|
1.0
|
OG
|
U:SER33
|
4.5
|
41.2
|
1.0
|
CB
|
U:TYR8
|
4.6
|
44.1
|
1.0
|
CA
|
U:CYS6
|
4.7
|
46.2
|
1.0
|
N
|
U:SER33
|
4.7
|
43.7
|
1.0
|
C
|
U:TYR8
|
4.9
|
45.6
|
1.0
|
N
|
U:GLY10
|
4.9
|
47.5
|
1.0
|
C
|
U:CYS9
|
4.9
|
47.0
|
1.0
|
CA
|
U:CYS36
|
4.9
|
45.8
|
1.0
|
CD2
|
U:TYR8
|
5.0
|
39.9
|
1.0
|
C
|
U:CYS32
|
5.0
|
42.9
|
1.0
|
|
Cadmium binding site 3 out
of 5 in 1vq8
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Cadmium Binding Sites List in 1vq8
Cadmium binding site 3 out
of 5 in the The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui
Mono view
Stereo pair view
|
A full contact list of Cadmium with other atoms in the Cd binding
site number 3 of The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
Z:Cd9203
b:59.1
occ:1.00
|
SG
|
Z:CYS60
|
2.2
|
46.9
|
1.0
|
SG
|
Z:CYS39
|
2.5
|
53.9
|
1.0
|
SG
|
Z:CYS57
|
2.6
|
57.0
|
1.0
|
SG
|
Z:CYS42
|
2.9
|
66.6
|
1.0
|
CB
|
Z:CYS39
|
3.1
|
54.9
|
1.0
|
CB
|
Z:CYS57
|
3.2
|
54.4
|
1.0
|
CB
|
Z:CYS60
|
3.4
|
50.0
|
1.0
|
CB
|
Z:CYS42
|
3.7
|
63.4
|
1.0
|
N
|
Z:CYS42
|
3.7
|
62.9
|
1.0
|
N
|
Z:CYS60
|
3.9
|
53.2
|
1.0
|
CB
|
Z:ASN41
|
4.1
|
59.1
|
1.0
|
CA
|
Z:CYS60
|
4.2
|
51.8
|
1.0
|
CA
|
Z:CYS42
|
4.3
|
63.0
|
1.0
|
CB
|
Z:TYR62
|
4.5
|
47.4
|
1.0
|
CD2
|
Z:TYR59
|
4.6
|
60.1
|
1.0
|
CA
|
Z:CYS39
|
4.6
|
55.9
|
1.0
|
CB
|
Z:TYR59
|
4.7
|
56.2
|
1.0
|
CA
|
Z:CYS57
|
4.8
|
53.0
|
1.0
|
C
|
Z:CYS42
|
4.8
|
63.4
|
1.0
|
C
|
Z:ASN41
|
4.8
|
62.0
|
1.0
|
ND2
|
Z:ASN41
|
4.8
|
58.9
|
1.0
|
C
|
Z:CYS60
|
4.9
|
52.1
|
1.0
|
CA
|
Z:ASN41
|
4.9
|
60.4
|
1.0
|
N
|
Z:TYR62
|
5.0
|
50.6
|
1.0
|
|
Cadmium binding site 4 out
of 5 in 1vq8
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Cadmium Binding Sites List in 1vq8
Cadmium binding site 4 out
of 5 in the The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui
Mono view
Stereo pair view
|
A full contact list of Cadmium with other atoms in the Cd binding
site number 4 of The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
1:Cd9202
b:55.3
occ:1.00
|
SG
|
1:CYS22
|
2.4
|
31.2
|
1.0
|
SG
|
1:CYS34
|
2.4
|
30.5
|
1.0
|
SG
|
1:CYS37
|
2.5
|
31.0
|
1.0
|
SG
|
1:CYS19
|
2.5
|
28.2
|
1.0
|
CB
|
1:CYS19
|
3.1
|
27.1
|
1.0
|
CB
|
1:CYS34
|
3.2
|
25.4
|
1.0
|
CB
|
1:CYS22
|
3.3
|
30.1
|
1.0
|
CB
|
1:CYS37
|
3.3
|
24.0
|
1.0
|
N
|
1:CYS22
|
3.7
|
33.0
|
1.0
|
N
|
1:CYS37
|
3.8
|
25.8
|
1.0
|
CA
|
1:CYS22
|
4.1
|
30.9
|
1.0
|
CA
|
1:CYS37
|
4.1
|
24.2
|
1.0
|
CB
|
1:PHE39
|
4.4
|
28.9
|
1.0
|
CA
|
1:CYS19
|
4.6
|
30.1
|
1.0
|
CA
|
1:CYS34
|
4.6
|
28.2
|
1.0
|
CB
|
1:ARG21
|
4.7
|
32.8
|
1.0
|
C
|
1:CYS37
|
4.7
|
25.2
|
1.0
|
C
|
1:ARG21
|
4.8
|
32.7
|
1.0
|
CB
|
1:SER36
|
4.8
|
24.9
|
1.0
|
C
|
1:CYS22
|
4.8
|
30.1
|
1.0
|
N
|
1:PHE39
|
4.8
|
29.1
|
1.0
|
C
|
1:SER36
|
4.8
|
28.0
|
1.0
|
N
|
1:GLY23
|
4.9
|
30.2
|
1.0
|
O
|
1:HOH9474
|
4.9
|
35.8
|
1.0
|
N
|
1:GLY38
|
4.9
|
26.2
|
1.0
|
CD
|
1:ARG21
|
5.0
|
32.6
|
1.0
|
|
Cadmium binding site 5 out
of 5 in 1vq8
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Cadmium Binding Sites List in 1vq8
Cadmium binding site 5 out
of 5 in the The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui
Mono view
Stereo pair view
|
A full contact list of Cadmium with other atoms in the Cd binding
site number 5 of The Structure of Ccda-Phe-Cap-Bio and the Antibiotic Sparsomycin Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
3:Cd9204
b:59.3
occ:1.00
|
SG
|
3:CYS71
|
2.3
|
55.9
|
1.0
|
SG
|
3:CYS11
|
2.4
|
49.2
|
1.0
|
SG
|
3:CYS74
|
2.4
|
58.6
|
1.0
|
SG
|
3:CYS14
|
2.5
|
60.0
|
1.0
|
CB
|
3:CYS71
|
3.0
|
55.2
|
1.0
|
CB
|
3:CYS14
|
3.3
|
54.9
|
1.0
|
CB
|
3:CYS74
|
3.4
|
57.0
|
1.0
|
CB
|
3:CYS11
|
3.5
|
47.4
|
1.0
|
N
|
3:CYS14
|
3.7
|
55.4
|
1.0
|
N
|
3:CYS74
|
4.0
|
57.3
|
1.0
|
CA
|
3:CYS14
|
4.1
|
55.4
|
1.0
|
OE1
|
3:GLN18
|
4.1
|
60.3
|
1.0
|
CA
|
3:CYS74
|
4.3
|
56.7
|
1.0
|
CB
|
3:HIS13
|
4.4
|
53.7
|
1.0
|
CA
|
3:CYS71
|
4.4
|
54.8
|
1.0
|
C
|
3:HIS13
|
4.7
|
55.0
|
1.0
|
O
|
3:HOH9497
|
4.8
|
90.6
|
1.0
|
CD
|
3:GLN18
|
4.8
|
56.8
|
1.0
|
CA
|
3:CYS11
|
4.9
|
47.9
|
1.0
|
CA
|
3:HIS13
|
5.0
|
53.7
|
1.0
|
|
Reference:
T.M.Schmeing,
K.S.Huang,
D.E.Kitchen,
S.A.Strobel,
T.A.Steitz.
Structural Insights Into the Roles of Water and the 2' Hydroxyl of the P Site Trna in the Peptidyl Transferase Reaction. Mol.Cell V. 20 437 2005.
ISSN: ISSN 1097-2765
PubMed: 16285925
DOI: 10.1016/J.MOLCEL.2005.09.006
Page generated: Fri Jul 19 14:19:37 2024
|