Zinc 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:
Zinc Binding Sites:
The binding sites of Zinc 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 Zinc atom.
In total 6 binding sites of Zinc 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 Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 1tny
Go back to
Zinc Binding Sites List in 1tny
Zinc 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 Zinc with other atoms in the Zn 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:Zn378
b:46.4
occ:1.00
|
OD2
|
B:ASP269
|
2.1
|
43.3
|
1.0
|
NE2
|
B:HIS321
|
2.2
|
49.5
|
1.0
|
SG
|
B:CYS271
|
2.3
|
50.0
|
1.0
|
SG
|
M:CYS8
|
2.3
|
47.8
|
1.0
|
OD1
|
B:ASP269
|
2.6
|
48.5
|
1.0
|
CG
|
B:ASP269
|
2.7
|
44.9
|
1.0
|
CE1
|
B:HIS321
|
3.1
|
46.2
|
1.0
|
CD2
|
B:HIS321
|
3.1
|
46.1
|
1.0
|
CB
|
B:CYS271
|
3.5
|
43.5
|
1.0
|
CB
|
M:CYS8
|
3.6
|
48.4
|
1.0
|
CB
|
B:ASP269
|
4.1
|
42.8
|
1.0
|
CB
|
B:LYS311
|
4.1
|
56.5
|
1.0
|
ND1
|
B:HIS321
|
4.2
|
47.0
|
1.0
|
CG
|
B:HIS321
|
4.3
|
46.0
|
1.0
|
N
|
B:CYS271
|
4.3
|
40.3
|
1.0
|
O
|
B:HOH416
|
4.4
|
52.2
|
1.0
|
CE
|
B:LYS311
|
4.5
|
68.8
|
1.0
|
CA
|
B:CYS271
|
4.5
|
41.4
|
1.0
|
CD2
|
B:LEU320
|
4.5
|
41.6
|
1.0
|
CE2
|
B:TYR272
|
4.6
|
37.4
|
1.0
|
CA
|
M:CYS8
|
4.9
|
49.8
|
1.0
|
NZ
|
B:LYS311
|
4.9
|
72.8
|
1.0
|
CA
|
B:LYS311
|
5.0
|
54.2
|
1.0
|
|
Zinc binding site 2 out
of 6 in 1tny
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Zinc Binding Sites List in 1tny
Zinc 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 Zinc with other atoms in the Zn 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:Zn378
b:44.9
occ:1.00
|
NE2
|
D:HIS321
|
2.1
|
43.1
|
1.0
|
OD2
|
D:ASP269
|
2.2
|
40.0
|
1.0
|
SG
|
D:CYS271
|
2.3
|
39.1
|
1.0
|
SG
|
N:CYS8
|
2.4
|
51.8
|
1.0
|
OD1
|
D:ASP269
|
2.6
|
40.4
|
1.0
|
CG
|
D:ASP269
|
2.7
|
38.1
|
1.0
|
CE1
|
D:HIS321
|
3.1
|
42.8
|
1.0
|
CD2
|
D:HIS321
|
3.1
|
44.8
|
1.0
|
CB
|
D:CYS271
|
3.4
|
35.9
|
1.0
|
CB
|
N:CYS8
|
3.4
|
52.6
|
1.0
|
CB
|
D:LYS311
|
4.1
|
54.8
|
1.0
|
CB
|
D:ASP269
|
4.2
|
36.8
|
1.0
|
ND1
|
D:HIS321
|
4.2
|
43.1
|
1.0
|
CG
|
D:HIS321
|
4.2
|
43.4
|
1.0
|
N
|
D:CYS271
|
4.2
|
34.0
|
1.0
|
CA
|
D:CYS271
|
4.4
|
34.8
|
1.0
|
CD2
|
D:LEU320
|
4.4
|
43.4
|
1.0
|
CE
|
D:LYS311
|
4.5
|
65.3
|
1.0
|
O
|
D:HOH445
|
4.6
|
40.4
|
1.0
|
CE2
|
D:TYR272
|
4.7
|
38.8
|
1.0
|
CA
|
N:CYS8
|
4.8
|
53.0
|
1.0
|
CA
|
D:LYS311
|
4.9
|
51.8
|
1.0
|
|
Zinc binding site 3 out
of 6 in 1tny
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Zinc Binding Sites List in 1tny
Zinc 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 Zinc with other atoms in the Zn 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:Zn378
b:44.4
occ:1.00
|
NE2
|
F:HIS321
|
2.1
|
39.5
|
1.0
|
OD2
|
F:ASP269
|
2.2
|
33.6
|
1.0
|
SG
|
O:CYS8
|
2.3
|
54.6
|
1.0
|
SG
|
F:CYS271
|
2.4
|
43.3
|
1.0
|
OD1
|
F:ASP269
|
2.6
|
38.0
|
1.0
|
CG
|
F:ASP269
|
2.7
|
34.4
|
1.0
|
CE1
|
F:HIS321
|
3.0
|
40.2
|
1.0
|
CD2
|
F:HIS321
|
3.0
|
38.0
|
1.0
|
CB
|
F:CYS271
|
3.4
|
34.9
|
1.0
|
CB
|
O:CYS8
|
3.6
|
54.6
|
1.0
|
CB
|
F:LYS311
|
4.1
|
53.6
|
1.0
|
ND1
|
F:HIS321
|
4.1
|
40.9
|
1.0
|
CG
|
F:HIS321
|
4.2
|
40.4
|
1.0
|
CB
|
F:ASP269
|
4.2
|
32.8
|
1.0
|
N
|
F:CYS271
|
4.2
|
35.0
|
1.0
|
O
|
F:HOH434
|
4.4
|
28.9
|
1.0
|
CA
|
F:CYS271
|
4.4
|
35.4
|
1.0
|
CD2
|
F:LEU320
|
4.4
|
41.6
|
1.0
|
CE
|
F:LYS311
|
4.5
|
67.8
|
1.0
|
CE2
|
F:TYR272
|
4.7
|
37.1
|
1.0
|
CA
|
F:LYS311
|
4.9
|
49.4
|
1.0
|
CA
|
O:CYS8
|
4.9
|
55.3
|
1.0
|
O
|
F:HOH412
|
5.0
|
40.4
|
1.0
|
NZ
|
F:LYS311
|
5.0
|
70.0
|
1.0
|
|
Zinc binding site 4 out
of 6 in 1tny
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Zinc Binding Sites List in 1tny
Zinc 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 Zinc with other atoms in the Zn 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:Zn378
b:51.6
occ:1.00
|
NE2
|
H:HIS321
|
2.1
|
62.1
|
1.0
|
OD2
|
H:ASP269
|
2.2
|
38.7
|
1.0
|
SG
|
H:CYS271
|
2.3
|
53.3
|
1.0
|
SG
|
P:CYS8
|
2.4
|
56.6
|
1.0
|
OD1
|
H:ASP269
|
2.6
|
49.1
|
1.0
|
CG
|
H:ASP269
|
2.7
|
43.6
|
1.0
|
CE1
|
H:HIS321
|
3.1
|
61.6
|
1.0
|
CD2
|
H:HIS321
|
3.1
|
62.1
|
1.0
|
CB
|
H:CYS271
|
3.4
|
48.6
|
1.0
|
CB
|
P:CYS8
|
3.6
|
58.5
|
1.0
|
CB
|
H:LYS311
|
4.1
|
72.7
|
1.0
|
CB
|
H:ASP269
|
4.2
|
43.1
|
1.0
|
ND1
|
H:HIS321
|
4.2
|
62.2
|
1.0
|
CG
|
H:HIS321
|
4.2
|
61.2
|
1.0
|
N
|
H:CYS271
|
4.2
|
45.3
|
1.0
|
CA
|
H:CYS271
|
4.4
|
46.1
|
1.0
|
CD2
|
H:LEU320
|
4.4
|
56.2
|
1.0
|
CE
|
H:LYS311
|
4.5
|
78.9
|
1.0
|
O
|
H:HOH417
|
4.5
|
33.9
|
1.0
|
CE2
|
H:TYR272
|
4.7
|
44.4
|
1.0
|
O
|
H:HOH398
|
4.7
|
45.3
|
1.0
|
CA
|
P:CYS8
|
4.9
|
59.7
|
1.0
|
CA
|
H:LYS311
|
5.0
|
71.8
|
1.0
|
NZ
|
H:LYS311
|
5.0
|
79.2
|
1.0
|
|
Zinc binding site 5 out
of 6 in 1tny
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Zinc Binding Sites List in 1tny
Zinc 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 Zinc with other atoms in the Zn 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:Zn378
b:44.0
occ:1.00
|
NE2
|
J:HIS321
|
2.2
|
45.7
|
1.0
|
OD2
|
J:ASP269
|
2.2
|
36.2
|
1.0
|
SG
|
J:CYS271
|
2.3
|
44.5
|
1.0
|
SG
|
Q:CYS8
|
2.4
|
44.8
|
1.0
|
OD1
|
J:ASP269
|
2.5
|
40.0
|
1.0
|
CG
|
J:ASP269
|
2.6
|
38.4
|
1.0
|
CD2
|
J:HIS321
|
3.1
|
44.7
|
1.0
|
CE1
|
J:HIS321
|
3.1
|
43.5
|
1.0
|
CB
|
J:CYS271
|
3.4
|
39.2
|
1.0
|
CB
|
Q:CYS8
|
3.6
|
47.5
|
1.0
|
CB
|
J:ASP269
|
4.1
|
36.8
|
1.0
|
CB
|
J:LYS311
|
4.1
|
50.6
|
1.0
|
N
|
J:CYS271
|
4.2
|
36.8
|
1.0
|
ND1
|
J:HIS321
|
4.2
|
44.5
|
1.0
|
CG
|
J:HIS321
|
4.2
|
43.5
|
1.0
|
O
|
J:HOH436
|
4.3
|
31.4
|
1.0
|
CA
|
J:CYS271
|
4.4
|
38.2
|
1.0
|
CD2
|
J:LEU320
|
4.5
|
39.0
|
1.0
|
CE
|
J:LYS311
|
4.5
|
65.4
|
1.0
|
CE2
|
J:TYR272
|
4.6
|
35.6
|
1.0
|
CA
|
J:LYS311
|
4.9
|
47.9
|
1.0
|
CA
|
Q:CYS8
|
5.0
|
48.6
|
1.0
|
CD2
|
J:TYR272
|
5.0
|
35.3
|
1.0
|
|
Zinc binding site 6 out
of 6 in 1tny
Go back to
Zinc Binding Sites List in 1tny
Zinc 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 Zinc with other atoms in the Zn 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:Zn378
b:38.5
occ:1.00
|
NE2
|
L:HIS321
|
2.1
|
35.8
|
1.0
|
OD2
|
L:ASP269
|
2.1
|
32.1
|
1.0
|
SG
|
L:CYS271
|
2.3
|
32.5
|
1.0
|
SG
|
R:CYS8
|
2.4
|
49.6
|
1.0
|
OD1
|
L:ASP269
|
2.5
|
33.7
|
1.0
|
CG
|
L:ASP269
|
2.6
|
32.6
|
1.0
|
CD2
|
L:HIS321
|
3.1
|
36.3
|
1.0
|
CE1
|
L:HIS321
|
3.1
|
35.5
|
1.0
|
CB
|
L:CYS271
|
3.4
|
27.1
|
1.0
|
CB
|
R:CYS8
|
3.5
|
50.6
|
1.0
|
CB
|
L:LYS311
|
4.1
|
40.6
|
1.0
|
CB
|
L:ASP269
|
4.1
|
30.7
|
1.0
|
ND1
|
L:HIS321
|
4.2
|
39.1
|
1.0
|
N
|
L:CYS271
|
4.2
|
27.8
|
1.0
|
CG
|
L:HIS321
|
4.2
|
38.2
|
1.0
|
CA
|
L:CYS271
|
4.4
|
27.0
|
1.0
|
O
|
L:HOH474
|
4.4
|
38.3
|
1.0
|
CE
|
L:LYS311
|
4.5
|
60.4
|
1.0
|
CD2
|
L:LEU320
|
4.5
|
34.4
|
1.0
|
CE2
|
L:TYR272
|
4.7
|
32.2
|
1.0
|
O
|
L:HOH433
|
4.8
|
35.7
|
1.0
|
CA
|
L:LYS311
|
4.9
|
37.8
|
1.0
|
CA
|
R:CYS8
|
4.9
|
51.5
|
1.0
|
CD2
|
L:TYR272
|
5.0
|
29.7
|
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
Page generated: Wed Oct 16 19:12:25 2024
|