Chlorine in PDB 5n5u: Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate

Enzymatic activity of Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate

All present enzymatic activity of Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate:
6.1.1.1;

Protein crystallography data

The structure of Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate, PDB code: 5n5u was solved by A.Schiefner, A.Skerra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.60
Space group P 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 52.582, 38.735, 82.034, 90.00, 90.28, 90.00
R / Rfree (%) 17.6 / 21.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate (pdb code 5n5u). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate, PDB code: 5n5u:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 5n5u

Go back to Chlorine Binding Sites List in 5n5u
Chlorine binding site 1 out of 3 in the Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:39.8
occ:1.00
 N A:HIS283 3.2 35.8 1.0
NH2 A:ARG257 3.3 55.1 1.0
CD A:ARG286 3.6 48.8 1.0
CD A:ARG257 3.7 58.5 1.0
CB A:HIS283 3.7 41.7 1.0
CG A:HIS283 3.8 46.7 1.0
CA A:LEU282 3.9 35.9 1.0
CB A:ARG286 3.9 38.9 1.0
CG A:ARG286 3.9 45.0 1.0
O A:GLU281 3.9 44.5 1.0
CA A:HIS283 4.0 37.1 1.0
C A:LEU282 4.0 34.7 1.0
CD1 A:LEU282 4.1 34.5 1.0
NE A:ARG286 4.2 55.3 1.0
ND1 A:HIS283 4.2 52.0 1.0
CD2 A:HIS283 4.2 48.6 1.0
CZ A:ARG257 4.3 59.4 1.0
NE A:ARG257 4.4 59.9 1.0
O A:PHE261 4.7 76.0 1.0
O A:HIS283 4.7 32.1 1.0
C A:GLU281 4.8 42.8 1.0
N A:LEU282 4.8 38.1 1.0
CE1 A:HIS283 4.8 53.6 1.0
NE2 A:HIS283 4.8 52.0 1.0
C A:HIS283 4.8 33.6 1.0
CB A:LEU282 4.8 33.2 1.0
CG A:ARG257 4.9 58.4 1.0
CG A:LEU282 4.9 32.9 1.0

Chlorine binding site 2 out of 3 in 5n5u

Go back to Chlorine Binding Sites List in 5n5u
Chlorine binding site 2 out of 3 in the Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl404

b:39.2
occ:1.00
 N A:VAL236 3.1 33.6 1.0
N A:GLU237 3.3 35.1 1.0
CA A:VAL236 3.9 32.7 1.0
CA A:VAL235 4.0 32.2 1.0
CB A:GLU237 4.0 43.7 1.0
C A:VAL235 4.0 31.9 1.0
CB A:VAL236 4.0 33.3 1.0
CE A:LYS278 4.0 57.3 1.0
C A:VAL236 4.1 34.0 1.0
CA A:GLU237 4.3 36.0 1.0
CG1 A:VAL235 4.3 33.0 1.0
O A:GLY234 4.4 38.7 1.0
CB A:VAL235 4.7 33.0 1.0
CG2 A:VAL236 4.7 34.6 1.0
CD A:LYS278 5.0 53.9 1.0

Chlorine binding site 3 out of 3 in 5n5u

Go back to Chlorine Binding Sites List in 5n5u
Chlorine binding site 3 out of 3 in the Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of P-Boronophenylalanyl Trna Synthetase in Complex with P- Boronophenylalanine and Adenosine Monophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl405

b:35.9
occ:0.50
 O A:HOH688 3.0 40.1 1.0
NH1 A:ARG131 3.4 44.7 1.0
CD A:ARG131 3.7 35.3 1.0
CB A:LEU127 3.8 26.3 1.0
CD1 A:LEU127 4.0 30.0 1.0
CD2 A:LEU127 4.2 25.9 1.0
CG A:LEU127 4.2 27.2 1.0
CZ A:ARG131 4.3 44.8 1.0
NE A:ARG131 4.5 39.2 1.0
CG A:ARG131 4.8 31.5 1.0

Reference:

A.Schiefner, L.Nastle, M.Landgraf, A.J.Reichert, A.Skerra. Structural Basis For the Specific Cotranslational Incorporation of P-Boronophenylalanine Into Biosynthetic Proteins. Biochemistry V. 57 2597 2018.
ISSN: ISSN 1520-4995
PubMed: 29668275
DOI: 10.1021/ACS.BIOCHEM.8B00171
Page generated: Sat Dec 12 12:08:32 2020

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