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Bromine in PDB 5ki8: Pseudo T4 Lysozyme Mutant - Y88PHE-Br

Enzymatic activity of Pseudo T4 Lysozyme Mutant - Y88PHE-Br

All present enzymatic activity of Pseudo T4 Lysozyme Mutant - Y88PHE-Br:
3.2.1.17;

Protein crystallography data

The structure of Pseudo T4 Lysozyme Mutant - Y88PHE-Br, PDB code: 5ki8 was solved by M.R.Scholfield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.70 / 1.55
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.013, 60.013, 95.945, 90.00, 90.00, 120.00
R / Rfree (%) 17.6 / 21

Bromine Binding Sites:

The binding sites of Bromine atom in the Pseudo T4 Lysozyme Mutant - Y88PHE-Br (pdb code 5ki8). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Pseudo T4 Lysozyme Mutant - Y88PHE-Br, PDB code: 5ki8:

Bromine binding site 1 out of 1 in 5ki8

Go back to Bromine Binding Sites List in 5ki8
Bromine binding site 1 out of 1 in the Pseudo T4 Lysozyme Mutant - Y88PHE-Br


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Pseudo T4 Lysozyme Mutant - Y88PHE-Br within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br88

b:27.0
occ:0.67
BR A:4BF88 0.0 27.0 0.7
CZ A:4BF88 1.9 21.3 1.0
CE1 A:4BF88 2.8 26.9 1.0
CE2 A:4BF88 2.8 22.3 1.0
C2 A:HED201 3.9 26.4 0.5
CD1 A:ILE100 4.1 19.9 1.0
CD1 A:4BF88 4.1 20.6 1.0
CD2 A:4BF88 4.1 18.8 1.0
CD A:ARG96 4.2 22.5 0.6
CD A:ARG96 4.3 22.6 0.4
CG1 A:VAL75 4.3 24.2 1.0
NE A:ARG96 4.3 23.9 0.4
S3 A:HED201 4.5 32.2 0.5
CB A:ARG96 4.6 18.7 0.6
CB A:ARG96 4.6 18.7 0.4
CG A:4BF88 4.7 19.1 1.0
O A:HOH301 4.7 32.3 1.0
CG2 A:VAL75 4.8 21.9 1.0
CG A:ARG96 4.8 19.2 0.6
O1 A:HED201 4.8 23.8 0.5
CG1 A:ILE100 4.9 16.3 1.0
C1 A:HED201 5.0 26.8 0.5

Reference:

M.R.Scholfield, M.C.Ford, A.C.Carlsson, H.Butta, R.A.Mehl, P.S.Ho. Structure-Energy Relationships of Halogen Bonds in Proteins. Biochemistry V. 56 2794 2017.
ISSN: ISSN 1520-4995
PubMed: 28345933
DOI: 10.1021/ACS.BIOCHEM.7B00022
Page generated: Thu Jul 11 00:08:06 2024

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