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Chlorine in PDB 3vbp: Crystal Structure of the D94N Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A

Enzymatic activity of Crystal Structure of the D94N Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A

All present enzymatic activity of Crystal Structure of the D94N Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A:
2.3.1.18;

Protein crystallography data

The structure of Crystal Structure of the D94N Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A, PDB code: 3vbp was solved by R.L.Kubiak, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.74 / 2.30
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 71.339, 71.339, 138.184, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 25.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the D94N Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A (pdb code 3vbp). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the D94N Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A, PDB code: 3vbp:

Chlorine binding site 1 out of 1 in 3vbp

Go back to Chlorine Binding Sites List in 3vbp
Chlorine binding site 1 out of 1 in the Crystal Structure of the D94N Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the D94N Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl190

b:28.0
occ:1.00
 NH1 A:ARG86 3.0 21.4 1.0
NH1 E:ARG86 3.1 23.0 1.0
NH1 C:ARG86 3.2 15.6 1.0
CG C:ARG86 3.5 20.2 1.0
CG E:ARG86 3.6 17.9 1.0
CD C:ARG86 3.6 19.6 1.0
CD E:ARG86 3.7 22.1 1.0
CD A:ARG86 3.8 19.6 1.0
CG A:ARG86 3.9 18.2 1.0
CD1 C:TYR65 3.9 19.7 1.0
CD1 A:TYR65 3.9 12.3 1.0
CD1 E:TYR65 4.0 14.9 1.0
CB A:TYR65 4.1 17.6 1.0
CB E:TYR65 4.1 18.7 1.0
CB C:TYR65 4.1 17.6 1.0
CZ A:ARG86 4.1 16.6 1.0
CZ E:ARG86 4.1 22.6 1.0
CG C:TYR65 4.1 20.4 1.0
CG A:TYR65 4.1 16.2 1.0
CZ C:ARG86 4.2 20.3 1.0
CG E:TYR65 4.2 17.7 1.0
NE C:ARG86 4.3 17.0 1.0
NE E:ARG86 4.4 17.1 1.0
NE A:ARG86 4.4 14.6 1.0
CE1 C:TYR65 4.7 19.8 1.0
CE1 A:TYR65 4.7 19.1 1.0
CE1 E:TYR65 4.7 14.3 1.0
CB C:ARG86 4.9 19.3 1.0
CB A:ARG86 4.9 18.7 1.0
CB E:ARG86 4.9 16.3 1.0
CD2 E:TYR65 5.0 19.8 1.0

Reference:

R.L.Kubiak, H.M.Holden. Structural Studies of Antd: An N-Acyltransferase Involved in the Biosynthesis of D-Anthrose. Biochemistry V. 51 867 2012.
ISSN: ISSN 0006-2960
PubMed: 22220494
DOI: 10.1021/BI201650C
Page generated: Sat Dec 12 10:17:08 2020

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