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Chlorine in PDB 1cla: Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase

Enzymatic activity of Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase

All present enzymatic activity of Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase:
2.3.1.28;

Protein crystallography data

The structure of Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase, PDB code: 1cla was solved by M.R.Gibbs, A.G.W.Leslie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.34
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 107.340, 107.340, 123.280, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1cla:

The structure of Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase also contains other interesting chemical elements:

Cobalt (Co) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase (pdb code 1cla). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase, PDB code: 1cla:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1cla

Go back to Chlorine Binding Sites List in 1cla
Chlorine binding site 1 out of 2 in the Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl221

b:21.8
occ:0.33
 CL1 A:CLM221 0.0 21.8 0.3
C1 A:CLM221 1.7 18.5 0.3
C2 A:CLM221 2.7 15.7 0.3
CL2 A:CLM221 2.9 21.4 0.3
O2 A:CLM221 3.0 15.8 0.3
N2 A:CLM221 3.7 14.6 0.3
ND2 A:ASN146 3.8 16.8 1.0
OE1 A:GLN92 4.1 17.2 1.0
C10 A:CLM221 4.2 18.1 0.3
C11 A:CLM221 4.2 15.8 0.3
CE2 A:PHE135 4.6 2.0 1.0
CZ A:PHE135 4.7 12.2 1.0
CG A:ASN146 4.7 14.3 1.0
C6 A:CLM221 4.8 15.9 0.3
C9 A:CLM221 4.8 19.5 0.3
C3 A:CLM221 5.0 14.7 0.3

Chlorine binding site 2 out of 2 in 1cla

Go back to Chlorine Binding Sites List in 1cla
Chlorine binding site 2 out of 2 in the Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl221

b:21.4
occ:0.33
 CL2 A:CLM221 0.0 21.4 0.3
C1 A:CLM221 1.8 18.5 0.3
C2 A:CLM221 2.6 15.7 0.3
CL1 A:CLM221 2.9 21.8 0.3
O2 A:CLM221 3.2 15.8 0.3
CB A:ALA105 3.3 2.0 1.0
N2 A:CLM221 3.4 14.6 0.3
CE2 A:PHE135 3.6 2.0 1.0
CZ A:PHE135 3.9 12.2 1.0
CE1 A:PHE103 4.3 14.8 1.0
OE1 A:GLN92 4.5 17.2 1.0
CD1 A:LEU134 4.6 7.9 1.0
CD2 A:PHE135 4.6 8.9 1.0
O A:HOH245 4.7 48.4 1.0
C3 A:CLM221 4.7 14.7 0.3
CA A:ALA105 4.7 4.7 1.0

Reference:

A.Lewendon, I.A.Murray, W.V.Shaw, M.R.Gibbs, A.G.Leslie. Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase. Biochemistry V. 29 2075 1990.
ISSN: ISSN 0006-2960
PubMed: 2109633
DOI: 10.1021/BI00460A016
Page generated: Sat Dec 12 08:33:05 2020

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