Chlorine in PDB 1tny: Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit
Enzymatic activity of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit
All present enzymatic activity of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit:
2.5.1.59;
Protein crystallography data
The structure of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit, PDB code: 1tny
was solved by
T.S Reid,
K.L.Terry,
P.J.Casey,
L.S.Beese,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.91 /
2.70
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
270.947,
264.007,
184.985,
90.00,
131.72,
90.00
|
R / Rfree (%)
|
19.3 /
21.2
|
Other elements in 1tny:
The structure of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit
(pdb code 1tny). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the
Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit, PDB code: 1tny:
Jump to Chlorine binding site number:
1;
2;
3;
4;
5;
6;
Chlorine binding site 1 out
of 6 in 1tny
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Chlorine Binding Sites List in 1tny
Chlorine binding site 1 out
of 6 in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl379
b:64.0
occ:1.00
|
N
|
B:GLN287
|
3.3
|
52.1
|
1.0
|
N
|
B:PHE286
|
3.3
|
50.7
|
1.0
|
C
|
B:LYS284
|
3.6
|
51.2
|
1.0
|
N
|
B:ILE285
|
3.7
|
50.7
|
1.0
|
CB
|
B:GLN287
|
3.8
|
52.2
|
1.0
|
NE2
|
B:GLN287
|
3.8
|
52.4
|
1.0
|
CB
|
B:PHE286
|
3.8
|
49.9
|
1.0
|
CA
|
B:LYS284
|
3.8
|
51.5
|
1.0
|
CG
|
B:GLN287
|
3.9
|
53.5
|
1.0
|
CA
|
B:PHE286
|
3.9
|
51.2
|
1.0
|
O
|
B:LYS284
|
3.9
|
51.8
|
1.0
|
CD
|
B:LYS281
|
4.0
|
55.9
|
1.0
|
C
|
B:ILE285
|
4.0
|
50.1
|
1.0
|
C
|
B:PHE286
|
4.1
|
52.0
|
1.0
|
CA
|
B:GLN287
|
4.1
|
52.9
|
1.0
|
CD
|
B:GLN287
|
4.1
|
54.1
|
1.0
|
CA
|
B:ILE285
|
4.2
|
50.0
|
1.0
|
CA
|
B:LYS281
|
4.4
|
51.6
|
1.0
|
O
|
B:LYS281
|
4.4
|
55.0
|
1.0
|
CE
|
B:LYS281
|
4.6
|
58.3
|
1.0
|
O
|
B:LEU280
|
4.6
|
49.1
|
1.0
|
NZ
|
B:LYS281
|
4.7
|
61.1
|
1.0
|
N
|
B:LYS284
|
4.8
|
51.8
|
1.0
|
CB
|
B:LYS284
|
4.8
|
53.9
|
1.0
|
C
|
B:LYS281
|
4.9
|
52.2
|
1.0
|
|
Chlorine binding site 2 out
of 6 in 1tny
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Chlorine Binding Sites List in 1tny
Chlorine binding site 2 out
of 6 in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cl379
b:49.8
occ:1.00
|
N
|
D:GLN287
|
3.1
|
37.7
|
1.0
|
N
|
D:PHE286
|
3.2
|
36.2
|
1.0
|
O
|
D:HOH404
|
3.5
|
42.0
|
1.0
|
C
|
D:LYS284
|
3.6
|
39.9
|
1.0
|
N
|
D:ILE285
|
3.6
|
36.5
|
1.0
|
CB
|
D:GLN287
|
3.7
|
38.7
|
1.0
|
CB
|
D:PHE286
|
3.7
|
31.7
|
1.0
|
CG
|
D:GLN287
|
3.7
|
44.1
|
1.0
|
CA
|
D:PHE286
|
3.8
|
35.6
|
1.0
|
CA
|
D:LYS284
|
3.9
|
42.2
|
1.0
|
C
|
D:PHE286
|
3.9
|
37.0
|
1.0
|
C
|
D:ILE285
|
3.9
|
36.1
|
1.0
|
O
|
D:LYS284
|
3.9
|
39.5
|
1.0
|
CA
|
D:GLN287
|
3.9
|
39.5
|
1.0
|
NE2
|
D:GLN287
|
4.1
|
46.6
|
1.0
|
CD
|
D:LYS281
|
4.1
|
47.5
|
1.0
|
CA
|
D:ILE285
|
4.1
|
35.1
|
1.0
|
CD
|
D:GLN287
|
4.2
|
46.6
|
1.0
|
CA
|
D:LYS281
|
4.4
|
40.3
|
1.0
|
O
|
D:LYS281
|
4.5
|
39.4
|
1.0
|
O
|
D:LEU280
|
4.6
|
39.6
|
1.0
|
N
|
D:LYS284
|
4.8
|
43.6
|
1.0
|
O
|
D:ILE285
|
4.9
|
35.0
|
1.0
|
NZ
|
D:LYS281
|
4.9
|
54.4
|
1.0
|
CG
|
D:PHE286
|
4.9
|
30.3
|
1.0
|
CE
|
D:LYS281
|
4.9
|
53.5
|
1.0
|
C
|
D:LYS281
|
4.9
|
39.4
|
1.0
|
CB
|
D:LYS284
|
4.9
|
43.9
|
1.0
|
CG
|
D:LYS281
|
5.0
|
45.0
|
1.0
|
|
Chlorine binding site 3 out
of 6 in 1tny
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Chlorine Binding Sites List in 1tny
Chlorine binding site 3 out
of 6 in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Cl379
b:49.9
occ:1.00
|
N
|
F:GLN287
|
3.2
|
39.7
|
1.0
|
N
|
F:PHE286
|
3.3
|
38.9
|
1.0
|
C
|
F:LYS284
|
3.5
|
37.9
|
1.0
|
N
|
F:ILE285
|
3.6
|
37.3
|
1.0
|
CB
|
F:GLN287
|
3.7
|
39.8
|
1.0
|
CG
|
F:GLN287
|
3.8
|
41.6
|
1.0
|
CA
|
F:LYS284
|
3.8
|
38.1
|
1.0
|
CB
|
F:PHE286
|
3.8
|
39.0
|
1.0
|
O
|
F:LYS284
|
3.9
|
37.9
|
1.0
|
CA
|
F:PHE286
|
3.9
|
38.5
|
1.0
|
NE2
|
F:GLN287
|
3.9
|
40.0
|
1.0
|
C
|
F:ILE285
|
4.0
|
38.2
|
1.0
|
C
|
F:PHE286
|
4.0
|
38.8
|
1.0
|
CA
|
F:GLN287
|
4.0
|
39.6
|
1.0
|
CA
|
F:ILE285
|
4.1
|
37.1
|
1.0
|
CD
|
F:GLN287
|
4.2
|
42.8
|
1.0
|
CD
|
F:LYS281
|
4.3
|
46.1
|
1.0
|
CA
|
F:LYS281
|
4.4
|
39.0
|
1.0
|
O
|
F:LYS281
|
4.5
|
41.3
|
1.0
|
CE
|
F:LYS281
|
4.6
|
48.8
|
1.0
|
O
|
F:LEU280
|
4.6
|
38.5
|
1.0
|
N
|
F:LYS284
|
4.8
|
39.3
|
1.0
|
CB
|
F:LYS284
|
4.8
|
37.8
|
1.0
|
CG
|
F:LYS281
|
4.9
|
42.3
|
1.0
|
C
|
F:LYS281
|
4.9
|
38.8
|
1.0
|
NZ
|
F:LYS281
|
5.0
|
50.7
|
1.0
|
O
|
F:ILE285
|
5.0
|
38.0
|
1.0
|
|
Chlorine binding site 4 out
of 6 in 1tny
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Chlorine Binding Sites List in 1tny
Chlorine binding site 4 out
of 6 in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 4 of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Cl379
b:54.5
occ:1.00
|
N
|
H:PHE286
|
3.1
|
46.2
|
1.0
|
N
|
H:GLN287
|
3.2
|
48.4
|
1.0
|
C
|
H:LYS284
|
3.4
|
46.1
|
1.0
|
N
|
H:ILE285
|
3.5
|
44.3
|
1.0
|
CB
|
H:PHE286
|
3.7
|
48.0
|
1.0
|
CA
|
H:LYS284
|
3.7
|
47.0
|
1.0
|
CA
|
H:PHE286
|
3.8
|
47.8
|
1.0
|
CB
|
H:GLN287
|
3.8
|
50.0
|
1.0
|
O
|
H:LYS284
|
3.8
|
46.4
|
1.0
|
CG
|
H:GLN287
|
3.9
|
52.6
|
1.0
|
NE2
|
H:GLN287
|
3.9
|
52.0
|
1.0
|
C
|
H:ILE285
|
3.9
|
45.1
|
1.0
|
C
|
H:PHE286
|
4.0
|
47.8
|
1.0
|
CA
|
H:ILE285
|
4.0
|
44.6
|
1.0
|
CA
|
H:GLN287
|
4.1
|
49.2
|
1.0
|
CD
|
H:LYS281
|
4.2
|
56.1
|
1.0
|
CD
|
H:GLN287
|
4.3
|
52.8
|
1.0
|
CA
|
H:LYS281
|
4.3
|
48.0
|
1.0
|
O
|
H:LYS281
|
4.4
|
48.9
|
1.0
|
O
|
H:LEU280
|
4.5
|
47.5
|
1.0
|
NZ
|
H:LYS281
|
4.6
|
61.4
|
1.0
|
N
|
H:LYS284
|
4.7
|
48.6
|
1.0
|
CB
|
H:LYS284
|
4.8
|
46.5
|
1.0
|
C
|
H:LYS281
|
4.8
|
48.1
|
1.0
|
CE
|
H:LYS281
|
4.8
|
61.0
|
1.0
|
O
|
H:ILE285
|
4.9
|
44.0
|
1.0
|
CG
|
H:PHE286
|
5.0
|
48.7
|
1.0
|
|
Chlorine binding site 5 out
of 6 in 1tny
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Chlorine Binding Sites List in 1tny
Chlorine binding site 5 out
of 6 in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 5 of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Cl379
b:68.0
occ:1.00
|
N
|
J:PHE286
|
3.0
|
51.7
|
1.0
|
N
|
J:GLN287
|
3.1
|
56.0
|
1.0
|
C
|
J:LYS284
|
3.5
|
52.6
|
1.0
|
N
|
J:ILE285
|
3.5
|
50.3
|
1.0
|
CB
|
J:PHE286
|
3.7
|
53.2
|
1.0
|
CA
|
J:PHE286
|
3.7
|
53.9
|
1.0
|
CB
|
J:GLN287
|
3.7
|
57.7
|
1.0
|
CA
|
J:LYS284
|
3.8
|
53.5
|
1.0
|
C
|
J:ILE285
|
3.8
|
50.6
|
1.0
|
O
|
J:LYS284
|
3.9
|
53.2
|
1.0
|
CG
|
J:GLN287
|
3.9
|
62.6
|
1.0
|
C
|
J:PHE286
|
3.9
|
54.5
|
1.0
|
CA
|
J:ILE285
|
4.0
|
50.0
|
1.0
|
CA
|
J:GLN287
|
4.0
|
56.1
|
1.0
|
CD
|
J:LYS281
|
4.1
|
60.9
|
1.0
|
NE2
|
J:GLN287
|
4.2
|
61.9
|
1.0
|
NZ
|
J:LYS281
|
4.2
|
66.1
|
1.0
|
CA
|
J:LYS281
|
4.3
|
52.2
|
1.0
|
CD
|
J:GLN287
|
4.4
|
63.2
|
1.0
|
O
|
J:LYS281
|
4.4
|
53.5
|
1.0
|
CE
|
J:LYS281
|
4.4
|
63.1
|
1.0
|
O
|
J:LEU280
|
4.5
|
52.8
|
1.0
|
N
|
J:LYS284
|
4.7
|
54.5
|
1.0
|
O
|
J:ILE285
|
4.8
|
50.8
|
1.0
|
CB
|
J:LYS284
|
4.9
|
54.9
|
1.0
|
C
|
J:LYS281
|
4.9
|
51.9
|
1.0
|
CG
|
J:PHE286
|
4.9
|
53.7
|
1.0
|
|
Chlorine binding site 6 out
of 6 in 1tny
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Chlorine Binding Sites List in 1tny
Chlorine binding site 6 out
of 6 in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 6 of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Frekkffcail Peptide Derived From the Heterotrimeric G Protein Gamma-2 Subunit within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Cl379
b:47.5
occ:1.00
|
N
|
L:PHE286
|
3.1
|
33.5
|
1.0
|
N
|
L:GLN287
|
3.3
|
36.5
|
1.0
|
C
|
L:LYS284
|
3.3
|
39.1
|
1.0
|
N
|
L:ILE285
|
3.4
|
36.0
|
1.0
|
CA
|
L:LYS284
|
3.6
|
40.4
|
1.0
|
CG
|
L:GLN287
|
3.7
|
43.1
|
1.0
|
O
|
L:LYS284
|
3.7
|
40.9
|
1.0
|
CB
|
L:PHE286
|
3.8
|
32.0
|
1.0
|
CA
|
L:PHE286
|
3.8
|
34.9
|
1.0
|
C
|
L:ILE285
|
3.8
|
34.3
|
1.0
|
NE2
|
L:GLN287
|
3.8
|
42.1
|
1.0
|
CB
|
L:GLN287
|
3.8
|
37.5
|
1.0
|
CA
|
L:ILE285
|
3.9
|
34.7
|
1.0
|
CE
|
L:LYS281
|
4.0
|
53.3
|
1.0
|
CD
|
L:LYS281
|
4.0
|
46.8
|
1.0
|
C
|
L:PHE286
|
4.0
|
35.5
|
1.0
|
CD
|
L:GLN287
|
4.1
|
42.7
|
1.0
|
CA
|
L:GLN287
|
4.1
|
37.8
|
1.0
|
CA
|
L:LYS281
|
4.3
|
37.1
|
1.0
|
O
|
L:LYS281
|
4.3
|
38.8
|
1.0
|
O
|
L:LEU280
|
4.4
|
35.9
|
1.0
|
N
|
L:LYS284
|
4.5
|
40.6
|
1.0
|
CB
|
L:LYS284
|
4.7
|
43.5
|
1.0
|
C
|
L:LYS281
|
4.8
|
37.5
|
1.0
|
O
|
L:ILE285
|
4.8
|
34.7
|
1.0
|
|
Reference:
T.S.Reid,
K.L.Terry,
P.J.Casey,
L.S.Beese.
Crystallographic Analysis of Caax Prenyltransferases Complexed with Substrates Defines Rules of Protein Substrate Selectivity. J.Mol.Biol. V. 343 417 2004.
ISSN: ISSN 0022-2836
PubMed: 15451670
DOI: 10.1016/J.JMB.2004.08.056
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