Cadmium in PDB 1vq6: The Structure of C-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui
Protein crystallography data
The structure of The Structure of C-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui, PDB code: 1vq6
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 /
2.70
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
212.050,
300.187,
573.987,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.4 /
23.3
|
Other elements in 1vq6:
The structure of The Structure of C-Hpmn and Cca-Phe-Cap-Bio 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 C-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui
(pdb code 1vq6). 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 C-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui, PDB code: 1vq6:
Jump to Cadmium binding site number:
1;
2;
3;
4;
5;
Cadmium binding site 1 out
of 5 in 1vq6
Go back to
Cadmium Binding Sites List in 1vq6
Cadmium binding site 1 out
of 5 in the The Structure of C-Hpmn and Cca-Phe-Cap-Bio 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 C-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cd9205
b:0.8
occ:1.00
|
ND1
|
O:HIS40
|
2.6
|
44.2
|
1.0
|
O
|
O:HOH5650
|
2.6
|
76.0
|
1.0
|
O
|
0:HOH6263
|
3.2
|
39.9
|
1.0
|
CE1
|
O:HIS40
|
3.4
|
44.3
|
1.0
|
CG
|
O:HIS40
|
3.6
|
43.4
|
1.0
|
CB
|
O:HIS40
|
3.9
|
46.5
|
1.0
|
CG
|
O:ARG37
|
4.3
|
56.0
|
1.0
|
O
|
O:HOH3002
|
4.4
|
53.6
|
1.0
|
NE2
|
O:HIS40
|
4.6
|
45.3
|
1.0
|
CB
|
O:ARG37
|
4.6
|
54.1
|
1.0
|
CZ
|
O:ARG37
|
4.7
|
54.2
|
1.0
|
NE
|
O:ARG37
|
4.7
|
56.7
|
1.0
|
CD2
|
O:HIS40
|
4.7
|
44.3
|
1.0
|
CA
|
O:ARG37
|
4.8
|
53.1
|
1.0
|
NH1
|
O:ARG37
|
4.9
|
52.7
|
1.0
|
CD
|
O:ARG37
|
5.0
|
56.5
|
1.0
|
|
Cadmium binding site 2 out
of 5 in 1vq6
Go back to
Cadmium Binding Sites List in 1vq6
Cadmium binding site 2 out
of 5 in the The Structure of C-Hpmn and Cca-Phe-Cap-Bio 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 C-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
U:Cd9201
b:78.4
occ:1.00
|
SG
|
U:CYS32
|
2.2
|
47.2
|
1.0
|
SG
|
U:CYS36
|
2.4
|
65.1
|
1.0
|
SG
|
U:CYS9
|
2.5
|
66.0
|
1.0
|
SG
|
U:CYS6
|
2.6
|
70.2
|
1.0
|
CB
|
U:CYS6
|
3.2
|
71.1
|
1.0
|
CB
|
U:CYS9
|
3.5
|
65.6
|
1.0
|
CB
|
U:CYS32
|
3.6
|
57.3
|
1.0
|
CB
|
U:CYS36
|
3.6
|
65.4
|
1.0
|
N
|
U:CYS9
|
3.9
|
67.1
|
1.0
|
N
|
U:CYS32
|
3.9
|
58.2
|
1.0
|
OG
|
U:SER33
|
4.3
|
62.7
|
1.0
|
CA
|
U:CYS9
|
4.3
|
67.1
|
1.0
|
CA
|
U:CYS32
|
4.3
|
58.7
|
1.0
|
OG1
|
U:THR11
|
4.4
|
74.5
|
1.0
|
N
|
U:SER33
|
4.5
|
61.6
|
1.0
|
CB
|
U:TYR8
|
4.5
|
63.7
|
1.0
|
CA
|
U:CYS6
|
4.7
|
71.0
|
1.0
|
C
|
U:CYS32
|
4.8
|
60.9
|
1.0
|
O
|
U:HOH6621
|
4.8
|
85.7
|
1.0
|
N
|
U:GLY10
|
4.9
|
68.0
|
1.0
|
C
|
U:TYR8
|
5.0
|
67.3
|
1.0
|
CA
|
U:CYS36
|
5.0
|
63.7
|
1.0
|
|
Cadmium binding site 3 out
of 5 in 1vq6
Go back to
Cadmium Binding Sites List in 1vq6
Cadmium binding site 3 out
of 5 in the The Structure of C-Hpmn and Cca-Phe-Cap-Bio 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 C-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
Z:Cd9203
b:76.1
occ:1.00
|
SG
|
Z:CYS39
|
2.2
|
72.1
|
1.0
|
SG
|
Z:CYS60
|
2.2
|
66.2
|
1.0
|
SG
|
Z:CYS57
|
2.3
|
73.1
|
1.0
|
SG
|
Z:CYS42
|
2.9
|
84.6
|
1.0
|
CB
|
Z:CYS57
|
3.2
|
74.7
|
1.0
|
CB
|
Z:CYS39
|
3.2
|
75.1
|
1.0
|
CB
|
Z:CYS60
|
3.4
|
69.4
|
1.0
|
N
|
Z:CYS42
|
3.5
|
81.5
|
1.0
|
CB
|
Z:CYS42
|
3.6
|
80.8
|
1.0
|
N
|
Z:CYS60
|
3.8
|
73.0
|
1.0
|
CB
|
Z:ASN41
|
3.9
|
84.1
|
1.0
|
CA
|
Z:CYS42
|
4.2
|
80.5
|
1.0
|
CA
|
Z:CYS60
|
4.2
|
70.7
|
1.0
|
CB
|
Z:TYR59
|
4.4
|
78.4
|
1.0
|
CD2
|
Z:TYR59
|
4.5
|
83.5
|
1.0
|
C
|
Z:ASN41
|
4.6
|
82.1
|
1.0
|
CB
|
Z:TYR62
|
4.6
|
63.7
|
1.0
|
CA
|
Z:CYS39
|
4.6
|
76.7
|
1.0
|
CA
|
Z:CYS57
|
4.7
|
73.2
|
1.0
|
CA
|
Z:ASN41
|
4.7
|
82.2
|
1.0
|
ND2
|
Z:ASN41
|
4.8
|
86.0
|
1.0
|
N
|
Z:ASN41
|
4.8
|
81.3
|
1.0
|
C
|
Z:CYS60
|
4.9
|
70.7
|
1.0
|
C
|
Z:TYR59
|
4.9
|
74.8
|
1.0
|
CG
|
Z:ASN41
|
4.9
|
85.5
|
1.0
|
C
|
Z:CYS39
|
4.9
|
78.1
|
1.0
|
C
|
Z:CYS42
|
4.9
|
79.3
|
1.0
|
O
|
Z:CYS39
|
5.0
|
79.7
|
1.0
|
N
|
Z:GLY43
|
5.0
|
78.2
|
1.0
|
CG
|
Z:TYR59
|
5.0
|
81.5
|
1.0
|
|
Cadmium binding site 4 out
of 5 in 1vq6
Go back to
Cadmium Binding Sites List in 1vq6
Cadmium binding site 4 out
of 5 in the The Structure of C-Hpmn and Cca-Phe-Cap-Bio 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 C-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
1:Cd9202
b:65.8
occ:1.00
|
SG
|
1:CYS22
|
2.4
|
42.3
|
1.0
|
SG
|
1:CYS37
|
2.4
|
40.4
|
1.0
|
SG
|
1:CYS34
|
2.5
|
44.3
|
1.0
|
SG
|
1:CYS19
|
2.6
|
45.4
|
1.0
|
CB
|
1:CYS19
|
3.1
|
42.6
|
1.0
|
CB
|
1:CYS22
|
3.2
|
40.8
|
1.0
|
CB
|
1:CYS34
|
3.2
|
38.5
|
1.0
|
CB
|
1:CYS37
|
3.3
|
39.1
|
1.0
|
N
|
1:CYS22
|
3.6
|
42.7
|
1.0
|
N
|
1:CYS37
|
3.7
|
39.0
|
1.0
|
CA
|
1:CYS22
|
3.9
|
42.1
|
1.0
|
CA
|
1:CYS37
|
4.1
|
39.0
|
1.0
|
CB
|
1:PHE39
|
4.3
|
39.0
|
1.0
|
CB
|
1:ARG21
|
4.5
|
41.0
|
1.0
|
CB
|
1:SER36
|
4.6
|
40.1
|
1.0
|
C
|
1:ARG21
|
4.6
|
43.3
|
1.0
|
CA
|
1:CYS19
|
4.6
|
44.4
|
1.0
|
C
|
1:CYS22
|
4.7
|
41.4
|
1.0
|
CA
|
1:CYS34
|
4.7
|
39.9
|
1.0
|
C
|
1:CYS37
|
4.8
|
37.6
|
1.0
|
O
|
1:HOH1020
|
4.8
|
47.1
|
1.0
|
C
|
1:SER36
|
4.8
|
39.8
|
1.0
|
N
|
1:GLY23
|
4.8
|
40.5
|
1.0
|
N
|
1:GLY38
|
4.9
|
36.8
|
1.0
|
CA
|
1:ARG21
|
4.9
|
42.9
|
1.0
|
N
|
1:PHE39
|
4.9
|
39.2
|
1.0
|
CD
|
1:ARG21
|
4.9
|
43.4
|
1.0
|
N
|
1:ARG21
|
5.0
|
42.6
|
1.0
|
|
Cadmium binding site 5 out
of 5 in 1vq6
Go back to
Cadmium Binding Sites List in 1vq6
Cadmium binding site 5 out
of 5 in the The Structure of C-Hpmn and Cca-Phe-Cap-Bio 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 C-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
3:Cd9204
b:64.1
occ:1.00
|
SG
|
3:CYS71
|
2.3
|
57.2
|
1.0
|
SG
|
3:CYS11
|
2.4
|
64.3
|
1.0
|
SG
|
3:CYS14
|
2.4
|
74.4
|
1.0
|
SG
|
3:CYS74
|
2.4
|
78.6
|
1.0
|
CB
|
3:CYS71
|
3.0
|
62.8
|
1.0
|
O
|
3:HOH9362
|
3.1
|
0.0
|
1.0
|
CB
|
3:CYS14
|
3.3
|
71.5
|
1.0
|
CB
|
3:CYS74
|
3.3
|
76.8
|
1.0
|
CB
|
3:CYS11
|
3.4
|
63.5
|
1.0
|
N
|
3:CYS14
|
3.7
|
70.9
|
1.0
|
N
|
3:CYS74
|
4.0
|
76.8
|
1.0
|
CA
|
3:CYS14
|
4.1
|
71.3
|
1.0
|
CA
|
3:CYS74
|
4.2
|
76.5
|
1.0
|
CA
|
3:CYS71
|
4.5
|
63.6
|
1.0
|
O
|
3:HOH9336
|
4.6
|
61.5
|
1.0
|
CB
|
3:HIS13
|
4.6
|
69.3
|
1.0
|
OE1
|
3:GLN18
|
4.7
|
83.8
|
1.0
|
CA
|
3:CYS11
|
4.8
|
62.8
|
1.0
|
C
|
3:HIS13
|
4.8
|
70.1
|
1.0
|
NE2
|
3:GLN18
|
4.9
|
81.8
|
1.0
|
CD
|
3:GLN18
|
4.9
|
79.8
|
1.0
|
C
|
3:CYS74
|
5.0
|
75.7
|
1.0
|
|
Reference:
T.M.Schmeing,
K.S.Huang,
S.A.Strobel,
T.A.Steitz.
An Induced-Fit Mechanism to Promote Peptide Bond Formation and Exclude Hydrolysis of Peptidyl-Trna. Nature V. 438 520 2005.
ISSN: ISSN 0028-0836
PubMed: 16306996
DOI: 10.1038/NATURE04152
Page generated: Fri Jul 19 14:18:52 2024
|