Chlorine in PDB 5vyt: Crystal Structure of the Wbkc N-Formyltransferase (F142A Variant) From Brucella Melitensis

All present enzymatic activity of Crystal Structure of the Wbkc N-Formyltransferase (F142A Variant) From Brucella Melitensis:
4.2.1.47;

The structure of Crystal Structure of the Wbkc N-Formyltransferase (F142A Variant) From Brucella Melitensis, PDB code: 5vyt was solved by A.S.Riegert, D.P.Chantigian, J.B.Thoden, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	67.315, 68.021, 236.035, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 26.8

The binding sites of Chlorine atom in the Crystal Structure of the Wbkc N-Formyltransferase (F142A Variant) From Brucella Melitensis (pdb code 5vyt). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the Wbkc N-Formyltransferase (F142A Variant) From Brucella Melitensis, PDB code: 5vyt:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the Wbkc N-Formyltransferase (F142A Variant) From Brucella Melitensis


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 Wbkc N-Formyltransferase (F142A Variant) From Brucella Melitensis within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl303 b:32.2 occ:1.00 N C:TYR198 4.1 23.3 1.0 CA C:SER197 4.1 22.7 1.0 CB C:TYR198 4.1 23.2 1.0 O C:ALA196 4.3 22.9 1.0 C C:SER197 4.3 23.1 1.0 C C:ALA196 4.3 22.9 1.0 CB C:ALA196 4.4 22.2 1.0 N C:SER197 4.5 22.9 1.0 CA C:TYR198 4.8 23.9 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the Wbkc N-Formyltransferase (F142A Variant) From Brucella Melitensis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Wbkc N-Formyltransferase (F142A Variant) From Brucella Melitensis within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl304 b:36.9 occ:1.00 CB C:ASN44 3.9 29.1 1.0 CD C:ARG45 4.0 30.0 1.0 N C:ASN44 4.1 24.6 1.0 CG C:ARG45 4.3 28.4 1.0 ND2 C:ASN44 4.4 38.7 1.0 N C:ARG45 4.4 24.8 1.0 CA C:ASN44 4.4 26.9 1.0 CG C:ASP43 4.5 17.3 1.0 OD1 C:ASP43 4.6 15.9 1.0 OD2 C:ASP43 4.7 16.3 1.0 CB C:ASP43 4.7 18.0 1.0 C C:ASN44 4.7 27.0 1.0 CD2 D:LEU55 4.7 22.9 1.0 CG C:ASN44 4.7 32.7 1.0 CD1 D:LEU55 4.8 22.0 1.0 OH C:TYR14 4.9 15.1 1.0 CB C:ARG45 5.0 26.5 1.0

A.S.Riegert, D.P.Chantigian, J.B.Thoden, P.A.Tipton, H.M.Holden. Biochemical Characterization of Wbkc, An N-Formyltransferase From Brucella Melitensis. Biochemistry V. 56 3657 2017.
ISSN: ISSN 1520-4995
PubMed: 28636341
DOI: 10.1021/ACS.BIOCHEM.7B00494