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Chlorine in PDB 8tfi: Trna 2'-Phosphotransferase (TPT1) From Pyrococcus Horikoshii

Protein crystallography data

The structure of Trna 2'-Phosphotransferase (TPT1) From Pyrococcus Horikoshii, PDB code: 8tfi was solved by A.Jacewicz, S.Dantuluri, S.Shuman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.17 / 1.97
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.464, 44.807, 124.736, 90, 90, 90
R / Rfree (%) 19.3 / 22.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Trna 2'-Phosphotransferase (TPT1) From Pyrococcus Horikoshii (pdb code 8tfi). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Trna 2'-Phosphotransferase (TPT1) From Pyrococcus Horikoshii, PDB code: 8tfi:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 8tfi

Go back to Chlorine Binding Sites List in 8tfi
Chlorine binding site 1 out of 2 in the Trna 2'-Phosphotransferase (TPT1) From Pyrococcus Horikoshii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Trna 2'-Phosphotransferase (TPT1) From Pyrococcus Horikoshii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl201

b:84.6
occ:1.00
OE2 A:GLU19 3.5 55.2 1.0
CG A:GLU19 3.5 50.7 1.0
O A:GLU19 3.7 47.7 1.0
CD A:GLU19 4.0 56.6 1.0
CE2 A:PHE20 4.1 55.7 1.0
CZ A:PHE20 4.1 53.0 1.0
O A:HOH351 4.3 66.8 1.0
CD2 A:PHE20 4.3 51.9 1.0
CE1 A:PHE20 4.3 54.7 1.0
C A:GLU19 4.5 57.0 1.0
CD1 A:PHE20 4.6 50.5 1.0
CG A:PHE20 4.6 50.3 1.0
CB A:GLU19 4.9 51.0 1.0

Chlorine binding site 2 out of 2 in 8tfi

Go back to Chlorine Binding Sites List in 8tfi
Chlorine binding site 2 out of 2 in the Trna 2'-Phosphotransferase (TPT1) From Pyrococcus Horikoshii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Trna 2'-Phosphotransferase (TPT1) From Pyrococcus Horikoshii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl202

b:64.3
occ:0.72
O A:HOH352 2.3 57.5 1.0
NE2 A:HIS119 2.8 60.4 1.0
N A:GLY75 3.1 43.5 1.0
CD A:ARG115 3.2 115.1 1.0
CE1 A:HIS119 3.6 67.4 1.0
CD2 A:HIS119 3.8 63.1 1.0
CA A:TYR74 3.9 41.6 1.0
CB A:TYR74 3.9 36.1 1.0
CG A:ARG115 3.9 104.1 1.0
CA A:GLY75 3.9 42.4 1.0
C A:TYR74 3.9 42.8 1.0
NE A:ARG115 4.0 118.7 1.0
NH1 A:ARG115 4.1 101.1 1.0
N A:HIS76 4.3 41.1 1.0
CD1 A:LEU82 4.3 47.9 1.0
CZ A:ARG115 4.3 103.4 1.0
CD2 A:TYR117 4.4 65.2 1.0
CB A:TYR117 4.4 56.6 1.0
C A:GLY75 4.5 48.4 1.0
CG2 A:ILE164 4.6 37.4 1.0
ND1 A:HIS119 4.8 71.6 1.0
CG A:TYR117 4.9 59.8 1.0
ND1 A:HIS76 4.9 42.6 1.0
CG A:HIS119 4.9 68.4 1.0

Reference:

A.Jacewicz, S.Dantuluri, S.Shuman. Structural Basis For TPT1-Catalyzed 2'-Po 4 Transfer From Rna and Nadp(H) to Nad. Proc.Natl.Acad.Sci.Usa V. 120 99120 2023.
ISSN: ESSN 1091-6490
PubMed: 37883434
DOI: 10.1073/PNAS.2312999120
Page generated: Thu Dec 28 03:32:23 2023

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