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Cobalt 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:

Chlorine (Cl) 2 atoms

Cobalt Binding Sites:

The binding sites of Cobalt 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 Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Evidence For Transition-State Stabilization By Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase, PDB code: 1cla:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 1cla

Go back to Cobalt Binding Sites List in 1cla
Cobalt 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 Cobalt with other atoms in the Co 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:Co222

b:6.7
occ:0.50
 OE1 A:GLU23 1.6 9.6 1.0
ND1 A:HIS27 2.1 9.2 1.0
CD A:GLU23 2.5 8.9 1.0
OE2 A:GLU23 2.8 10.4 1.0
CE1 A:HIS27 3.1 13.3 1.0
CG A:HIS27 3.1 12.2 1.0
CB A:HIS27 3.4 7.7 1.0
CG A:GLU23 3.9 8.7 1.0
O A:HOH267 4.0 42.5 1.0
NE2 A:HIS27 4.2 14.9 1.0
CD2 A:HIS27 4.2 5.5 1.0
O A:HOH256 4.6 21.1 1.0
O A:HOH268 4.8 24.1 1.0
CA A:HIS27 5.0 7.9 1.0

Cobalt binding site 2 out of 2 in 1cla

Go back to Cobalt Binding Sites List in 1cla
Cobalt 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 Cobalt with other atoms in the Co 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:Co223

b:35.2
occ:0.50
 O A:HOH341 1.4 37.5 0.5
O A:HOH282 2.1 25.7 1.0
O A:ASN68 3.9 12.6 1.0
O A:HOH300 4.2 46.8 1.0
O A:ASP87 4.3 16.4 1.0
O A:HOH371 4.8 79.8 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: Sun Jul 13 17:26:02 2025

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