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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:

Chlorine (Cl) 6 atoms

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

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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 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 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 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 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

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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

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