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Chlorine in PDB 6rz2: Sall with Chloroadenosine

Enzymatic activity of Sall with Chloroadenosine

All present enzymatic activity of Sall with Chloroadenosine:
2.5.1.94;

Protein crystallography data

The structure of Sall with Chloroadenosine, PDB code: 6rz2 was solved by I.Mckean, A.Frese, A.Cuetos, G.Burley, G.Grogan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.47 / 1.77
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.842, 111.579, 165.565, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 20.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Sall with Chloroadenosine (pdb code 6rz2). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Sall with Chloroadenosine, PDB code: 6rz2:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 6rz2

Go back to Chlorine Binding Sites List in 6rz2
Chlorine binding site 1 out of 3 in the Sall with Chloroadenosine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Sall with Chloroadenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl301

b:26.3
occ:1.00
CL B:5CD301 0.0 26.3 1.0
C5' B:5CD301 1.8 30.3 1.0
C4' B:5CD301 2.7 26.2 1.0
N B:GLY131 3.2 17.8 1.0
N B:TYR130 3.5 17.2 1.0
CB B:THR75 3.5 18.8 1.0
O4' B:5CD301 3.6 22.7 1.0
CA B:TRP129 3.6 19.1 1.0
OG1 B:THR75 3.7 19.9 1.0
CD1 B:TRP129 3.7 21.5 1.0
C B:TRP129 3.8 17.5 1.0
CB B:TYR72 3.8 16.9 1.0
O B:THR128 3.8 22.0 1.0
CG2 B:THR75 3.9 19.3 1.0
CA B:GLY131 3.9 16.7 1.0
C3' B:5CD301 4.0 23.5 1.0
O B:TYR72 4.0 18.3 1.0
C B:TYR130 4.2 17.3 1.0
CA B:TYR130 4.3 16.6 1.0
N B:TRP129 4.3 18.2 1.0
CD1 B:TYR70 4.3 16.1 1.0
O3' B:5CD301 4.3 20.5 1.0
C B:THR128 4.3 19.5 1.0
CE1 B:TYR70 4.4 17.2 1.0
CG B:TYR72 4.4 16.0 1.0
CD2 B:TYR72 4.4 16.9 1.0
CB B:TYR130 4.5 19.7 1.0
CG B:TRP129 4.6 20.1 1.0
CB B:TRP129 4.7 20.6 1.0
C1' B:5CD301 4.7 22.9 1.0
NE1 B:TRP129 4.7 22.2 1.0
O B:TRP129 4.7 20.2 1.0
C B:TYR72 4.8 16.8 1.0
CA B:TYR72 4.8 16.5 1.0
CA B:THR75 4.9 18.8 1.0

Chlorine binding site 2 out of 3 in 6rz2

Go back to Chlorine Binding Sites List in 6rz2
Chlorine binding site 2 out of 3 in the Sall with Chloroadenosine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Sall with Chloroadenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl302

b:23.2
occ:1.00
CL B:5CD302 0.0 23.2 1.0
C5' B:5CD302 1.8 31.1 1.0
C4' B:5CD302 2.7 27.3 1.0
N C:GLY131 3.2 17.7 1.0
N C:TYR130 3.5 15.8 1.0
CB C:THR75 3.6 15.2 1.0
O4' B:5CD302 3.6 22.8 1.0
CA C:TRP129 3.6 16.9 1.0
OG1 C:THR75 3.7 15.7 1.0
CD1 C:TRP129 3.7 18.1 1.0
CB C:TYR72 3.8 18.0 1.0
C C:TRP129 3.8 17.5 1.0
O C:THR128 3.9 17.7 1.0
CA C:GLY131 3.9 16.3 1.0
CG2 C:THR75 3.9 14.5 1.0
C3' B:5CD302 4.0 22.6 1.0
O C:TYR72 4.1 14.6 1.0
C C:TYR130 4.2 17.0 1.0
O3' B:5CD302 4.2 21.5 1.0
CD1 C:TYR70 4.2 17.3 1.0
CA C:TYR130 4.3 16.5 1.0
N C:TRP129 4.3 17.1 1.0
CE1 C:TYR70 4.3 17.4 1.0
CG C:TYR72 4.3 16.8 1.0
CD2 C:TYR72 4.4 17.1 1.0
C C:THR128 4.4 18.0 1.0
O B:HOH578 4.5 44.7 1.0
CB C:TYR130 4.6 16.4 1.0
CG C:TRP129 4.6 18.0 1.0
C1' B:5CD302 4.7 21.0 1.0
CB C:TRP129 4.7 17.8 1.0
NE1 C:TRP129 4.7 19.5 1.0
O C:TRP129 4.8 17.2 1.0
C C:TYR72 4.8 15.8 1.0
CA C:TYR72 4.8 16.6 1.0
CA C:THR75 4.9 17.0 1.0

Chlorine binding site 3 out of 3 in 6rz2

Go back to Chlorine Binding Sites List in 6rz2
Chlorine binding site 3 out of 3 in the Sall with Chloroadenosine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Sall with Chloroadenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl301

b:22.5
occ:1.00
CL C:5CD301 0.0 22.5 1.0
C5' C:5CD301 1.8 29.4 1.0
C4' C:5CD301 2.8 25.2 1.0
N A:GLY131 3.2 16.1 1.0
N A:TYR130 3.5 17.5 1.0
CB A:THR75 3.5 16.8 1.0
O4' C:5CD301 3.6 23.4 1.0
CA A:TRP129 3.6 17.6 1.0
OG1 A:THR75 3.6 16.1 1.0
CD1 A:TRP129 3.7 18.8 1.0
CB A:TYR72 3.8 17.9 1.0
C A:TRP129 3.8 18.0 1.0
O A:THR128 3.8 17.2 1.0
CG2 A:THR75 3.9 17.3 1.0
CA A:GLY131 3.9 16.0 1.0
C3' C:5CD301 4.0 22.6 1.0
O A:TYR72 4.1 15.7 1.0
C A:TYR130 4.1 15.5 1.0
CA A:TYR130 4.2 16.6 1.0
O3' C:5CD301 4.3 21.3 1.0
N A:TRP129 4.3 17.9 1.0
CD1 A:TYR70 4.3 15.1 1.0
CG A:TYR72 4.3 16.4 1.0
C A:THR128 4.4 18.4 1.0
CE1 A:TYR70 4.4 16.3 1.0
CD2 A:TYR72 4.4 16.4 1.0
CB A:TYR130 4.5 16.9 1.0
CG A:TRP129 4.6 18.4 1.0
O C:HOH582 4.6 50.5 1.0
C1' C:5CD301 4.7 21.4 1.0
CB A:TRP129 4.7 17.2 1.0
O A:TRP129 4.7 15.6 1.0
NE1 A:TRP129 4.7 20.1 1.0
C A:TYR72 4.8 15.8 1.0
CA A:TYR72 4.8 15.3 1.0
CA A:THR75 4.9 16.9 1.0

Reference:

I.J.W.Mckean, J.C.Sadler, A.Cuetos, A.Frese, L.D.Humphreys, G.Grogan, P.A.Hoskisson, G.A.Burley. S-Adenosyl Methionine Cofactor Modifications Enhance the Biocatalytic Repertoire of Small Molecule C-Alkylation. Angew.Chem.Int.Ed.Engl. V. 58 17583 2019.
ISSN: ESSN 1521-3773
PubMed: 31573135
DOI: 10.1002/ANIE.201908681
Page generated: Sat Jul 12 19:33:55 2025

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