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Chlorine in PDB 3g7u: Crystal Structure of Putative Dna Modification Methyltransferase Encoded Within Prophage Cp-933R (E.Coli)

Enzymatic activity of Crystal Structure of Putative Dna Modification Methyltransferase Encoded Within Prophage Cp-933R (E.Coli)

All present enzymatic activity of Crystal Structure of Putative Dna Modification Methyltransferase Encoded Within Prophage Cp-933R (E.Coli):
2.1.1.37;

Protein crystallography data

The structure of Crystal Structure of Putative Dna Modification Methyltransferase Encoded Within Prophage Cp-933R (E.Coli), PDB code: 3g7u was solved by Y.Patskovsky, U.A.Ramagopal, R.Toro, M.Gilmore, M.Iizuka, J.M.Sauder, S.K.Burley, S.C.Almo, New York Sgx Research Center For Structuralgenomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.75
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 79.436, 79.436, 126.539, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 21.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Putative Dna Modification Methyltransferase Encoded Within Prophage Cp-933R (E.Coli) (pdb code 3g7u). 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 Putative Dna Modification Methyltransferase Encoded Within Prophage Cp-933R (E.Coli), PDB code: 3g7u:

Chlorine binding site 1 out of 1 in 3g7u

Go back to Chlorine Binding Sites List in 3g7u
Chlorine binding site 1 out of 1 in the Crystal Structure of Putative Dna Modification Methyltransferase Encoded Within Prophage Cp-933R (E.Coli)


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 Putative Dna Modification Methyltransferase Encoded Within Prophage Cp-933R (E.Coli) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:39.9
occ:1.00
 O A:HOH502 3.0 38.9 1.0
NE A:ARG162 3.0 25.6 0.5
N A:SER350 3.1 20.0 1.0
NH2 A:ARG162 3.6 24.9 0.5
CD A:ARG160 3.7 39.3 0.5
CB A:SER350 3.7 21.9 1.0
CZ A:ARG162 3.7 23.9 0.5
CD A:ARG162 3.8 29.7 0.5
CG1 A:VAL349 3.8 26.2 1.0
CA A:VAL349 4.0 20.4 1.0
CD A:ARG162 4.0 27.8 0.5
CG A:ARG160 4.0 37.6 0.5
C A:VAL349 4.0 19.1 1.0
CA A:SER350 4.0 17.2 1.0
CG A:ARG160 4.2 40.7 0.5
CG2 A:VAL353 4.3 26.5 1.0
CG A:ARG162 4.3 31.9 0.5
CB A:ARG162 4.3 30.1 0.5
CB A:VAL353 4.3 27.7 1.0
CD A:ARG160 4.4 38.3 0.5
CB A:ALA151 4.4 24.8 1.0
CB A:ARG162 4.4 30.4 0.5
CB A:VAL349 4.5 22.9 1.0
CG1 A:VAL353 4.6 30.5 1.0
NE2 A:GLN326 4.6 50.2 1.0
NH2 A:ARG162 4.7 32.1 0.5
NE A:ARG162 4.7 31.1 0.5
O A:SER350 4.8 25.3 1.0
NE A:ARG160 4.8 46.8 0.5
CG A:ARG162 4.9 32.8 0.5
O A:SER348 4.9 25.6 1.0
NH2 A:ARG160 4.9 47.5 0.5
C A:SER350 5.0 20.3 1.0

Reference:

Y.Patskovsky, U.A.Ramagopal, R.Toro, M.Gilmore, M.Iizuka, J.M.Sauder, S.K.Burley, S.C.Almo. Crystal Structure of Dna Modification Methyltransferase Encoded Within Prophage Cp-933R (E.Coli) To Be Published.
Page generated: Sat Dec 12 09:43:52 2020

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