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Chlorine in PDB 1tno: Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Kkksktkcvim Peptide Derived From K- RAS4B

Enzymatic activity of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Kkksktkcvim Peptide Derived From K- RAS4B

All present enzymatic activity of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Kkksktkcvim Peptide Derived From K- RAS4B:
2.5.1.59;

Protein crystallography data

The structure of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Kkksktkcvim Peptide Derived From K- RAS4B, PDB code: 1tno 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) 29.98 / 2.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 272.531, 268.484, 185.940, 90.00, 131.48, 90.00
R / Rfree (%) 19.4 / 21.1

Other elements in 1tno:

The structure of Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Kkksktkcvim Peptide Derived From K- RAS4B also contains other interesting chemical elements:

Zinc (Zn) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Kkksktkcvim Peptide Derived From K- RAS4B (pdb code 1tno). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Kkksktkcvim Peptide Derived From K- RAS4B, PDB code: 1tno:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 1tno

Go back to Chlorine Binding Sites List in 1tno
Chlorine binding site 1 out of 4 in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Kkksktkcvim Peptide Derived From K- RAS4B


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 Kkksktkcvim Peptide Derived From K- RAS4B within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl379

b:62.3
occ:1.00
 N D:GLN287 3.2 48.3 1.0
N D:PHE286 3.2 46.8 1.0
C D:LYS284 3.5 50.5 1.0
CG D:GLN287 3.6 54.6 1.0
N D:ILE285 3.6 47.1 1.0
CB D:GLN287 3.7 49.3 1.0
CB D:PHE286 3.8 42.3 1.0
CA D:LYS284 3.8 52.8 1.0
CA D:PHE286 3.9 46.2 1.0
O D:LYS284 3.9 50.1 1.0
NE2 D:GLN287 3.9 57.2 1.0
C D:ILE285 4.0 46.7 1.0
C D:PHE286 4.0 47.6 1.0
CA D:GLN287 4.1 50.1 1.0
CA D:ILE285 4.1 45.7 1.0
CD D:GLN287 4.2 57.2 1.0
CD D:LYS281 4.3 58.1 1.0
CA D:LYS281 4.5 50.9 1.0
O D:LYS281 4.5 50.0 1.0
O D:LEU280 4.7 50.2 1.0
N D:LYS284 4.8 54.2 1.0
CB D:LYS284 4.8 54.5 1.0
O D:ILE285 5.0 45.6 1.0

Chlorine binding site 2 out of 4 in 1tno

Go back to Chlorine Binding Sites List in 1tno
Chlorine binding site 2 out of 4 in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Kkksktkcvim Peptide Derived From K- RAS4B


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 Kkksktkcvim Peptide Derived From K- RAS4B within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl379

b:55.2
occ:1.00
 N F:PHE286 3.3 49.2 1.0
N F:GLN287 3.3 50.0 1.0
C F:LYS284 3.6 48.2 1.0
N F:ILE285 3.7 47.6 1.0
CA F:LYS284 3.8 48.5 1.0
CB F:GLN287 3.8 50.1 1.0
CB F:PHE286 3.8 49.4 1.0
CG F:GLN287 3.9 51.9 1.0
CA F:PHE286 3.9 48.8 1.0
O F:LYS284 3.9 48.2 1.0
NE2 F:GLN287 4.0 50.3 1.0
C F:ILE285 4.1 48.5 1.0
C F:PHE286 4.1 49.1 1.0
CA F:GLN287 4.2 49.9 1.0
CA F:ILE285 4.2 47.4 1.0
CD F:GLN287 4.3 53.1 1.0
CD F:LYS281 4.3 56.4 1.0
CA F:LYS281 4.5 49.3 1.0
O F:LYS281 4.5 51.6 1.0
O F:LEU280 4.6 48.8 1.0
CE F:LYS281 4.7 59.1 1.0
N F:LYS284 4.8 49.6 1.0
CB F:LYS284 4.8 48.1 1.0
C F:LYS281 5.0 49.1 1.0
CG F:LYS281 5.0 52.6 1.0

Chlorine binding site 3 out of 4 in 1tno

Go back to Chlorine Binding Sites List in 1tno
Chlorine binding site 3 out of 4 in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Kkksktkcvim Peptide Derived From K- RAS4B


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 Kkksktkcvim Peptide Derived From K- RAS4B within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Cl379

b:69.3
occ:1.00
 N H:PHE286 3.2 57.4 1.0
N H:GLN287 3.3 59.6 1.0
C H:LYS284 3.5 57.3 1.0
N H:ILE285 3.6 55.5 1.0
CB H:PHE286 3.7 59.1 1.0
CA H:LYS284 3.8 58.2 1.0
CA H:PHE286 3.8 59.0 1.0
CG H:GLN287 3.8 63.7 1.0
CB H:GLN287 3.9 61.1 1.0
O H:LYS284 3.9 57.5 1.0
C H:ILE285 3.9 56.3 1.0
NE2 H:GLN287 4.0 63.1 1.0
C H:PHE286 4.0 59.0 1.0
CA H:ILE285 4.1 55.7 1.0
CD H:LYS281 4.1 67.2 1.0
CA H:GLN287 4.2 60.3 1.0
CD H:GLN287 4.3 64.0 1.0
CA H:LYS281 4.3 59.2 1.0
O H:LYS281 4.4 60.1 1.0
O H:LEU280 4.5 58.6 1.0
NZ H:LYS281 4.6 72.5 1.0
N H:LYS284 4.7 59.8 1.0
CE H:LYS281 4.8 72.1 1.0
CB H:LYS284 4.8 57.7 1.0
C H:LYS281 4.9 59.2 1.0
CG H:PHE286 5.0 59.9 1.0
O H:ILE285 5.0 55.1 1.0

Chlorine binding site 4 out of 4 in 1tno

Go back to Chlorine Binding Sites List in 1tno
Chlorine binding site 4 out of 4 in the Rat Protein Geranylgeranyltransferase Type-I Complexed with A Ggpp Analog and A Kkksktkcvim Peptide Derived From K- RAS4B


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 Kkksktkcvim Peptide Derived From K- RAS4B within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Cl379

b:59.7
occ:1.00
 N L:PHE286 3.2 44.3 1.0
N L:GLN287 3.3 47.4 1.0
C L:LYS284 3.4 50.0 1.0
N L:ILE285 3.5 46.8 1.0
CG L:GLN287 3.6 54.0 1.0
CA L:LYS284 3.7 51.2 1.0
CB L:PHE286 3.8 42.8 1.0
NE2 L:GLN287 3.8 53.0 1.0
O L:LYS284 3.8 51.7 1.0
CB L:GLN287 3.8 48.4 1.0
CD L:LYS281 3.9 57.6 1.0
CA L:PHE286 3.9 45.7 1.0
C L:ILE285 3.9 45.2 1.0
CA L:ILE285 4.0 45.5 1.0
CD L:GLN287 4.0 53.5 1.0
C L:PHE286 4.1 46.3 1.0
CA L:GLN287 4.2 48.7 1.0
O L:LYS281 4.4 49.7 1.0
CA L:LYS281 4.4 47.9 1.0
CE L:LYS281 4.5 64.2 1.0
O L:LEU280 4.5 46.7 1.0
N L:LYS284 4.6 51.4 1.0
CB L:LYS284 4.7 54.3 1.0
C L:LYS281 4.9 48.3 1.0
O L:ILE285 4.9 45.5 1.0
NZ L:LYS281 4.9 64.8 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: Sat Dec 12 08:50:14 2020

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