Chlorine in PDB 1d7o: Crystal Structure of Brassica Napus Enoyl Acyl Carrier Protein Reductase Complexed with Nad and Triclosan

All present enzymatic activity of Crystal Structure of Brassica Napus Enoyl Acyl Carrier Protein Reductase Complexed with Nad and Triclosan:
1.3.1.9;

The structure of Crystal Structure of Brassica Napus Enoyl Acyl Carrier Protein Reductase Complexed with Nad and Triclosan, PDB code: 1d7o was solved by A.Roujeinikova, C.Levy, S.Rowsell, S.Sedelnikova, P.J.Baker, C.A.Minshull, A.Mistry, J.G.Colls, R.Camble, A.R.Stuitje, A.R.Slabas, J.B.Rafferty, R.A.Pauptit, R.Viner, D.W.Rice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.90
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	70.500, 70.500, 118.000, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the Crystal Structure of Brassica Napus Enoyl Acyl Carrier Protein Reductase Complexed with Nad and Triclosan (pdb code 1d7o). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Brassica Napus Enoyl Acyl Carrier Protein Reductase Complexed with Nad and Triclosan, PDB code: 1d7o:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Brassica Napus Enoyl Acyl Carrier Protein Reductase Complexed with Nad and Triclosan


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 Brassica Napus Enoyl Acyl Carrier Protein Reductase Complexed with Nad and Triclosan within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:33.9 occ:1.00 CL14 A:TCL502 0.0 33.9 1.0 C2 A:TCL502 1.8 32.0 1.0 C1 A:TCL502 2.7 17.9 1.0 C3 A:TCL502 2.7 21.4 1.0 CE2 A:PHE246 3.6 42.3 1.0 CZ A:TYR188 3.7 25.5 1.0 CE1 A:TYR188 3.7 18.2 1.0 C6 A:TCL502 3.9 25.1 1.0 C4 A:TCL502 4.0 26.2 1.0 C4N A:NAD501 4.0 23.2 1.0 OH A:TYR188 4.0 26.0 1.0 O7N A:NAD501 4.0 31.2 1.0 CE2 A:TYR188 4.1 18.5 1.0 CD1 A:TYR188 4.2 17.8 1.0 CZ A:PHE246 4.3 37.4 1.0 CA A:PRO235 4.4 21.2 1.0 C5 A:TCL502 4.4 33.7 1.0 CB A:PRO235 4.4 19.8 1.0 CD2 A:TYR188 4.5 14.3 1.0 C3N A:NAD501 4.5 23.1 1.0 C7N A:NAD501 4.5 30.6 1.0 CG A:TYR188 4.5 13.7 1.0 CD2 A:PHE246 4.6 39.8 1.0 C5N A:NAD501 4.8 22.0 1.0 N A:PRO235 4.9 23.6 1.0 CE1 A:TYR198 4.9 22.6 1.0 CG1 A:ILE247 5.0 46.4 1.0 O17 A:TCL502 5.0 23.2 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Brassica Napus Enoyl Acyl Carrier Protein Reductase Complexed with Nad and Triclosan


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 Brassica Napus Enoyl Acyl Carrier Protein Reductase Complexed with Nad and Triclosan within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:39.9 occ:1.00 CL15 A:TCL502 0.0 39.9 1.0 C11 A:TCL502 1.7 50.5 1.0 C10 A:TCL502 2.7 19.8 1.0 C12 A:TCL502 2.7 64.0 1.0 N A:GLY140 3.0 23.1 1.0 O A:GLY140 3.6 29.4 1.0 C A:ASN139 3.6 24.0 1.0 CA A:GLY140 3.7 25.4 1.0 CA A:ASN139 3.8 20.7 1.0 C9 A:TCL502 4.0 45.4 1.0 C13 A:TCL502 4.0 34.6 1.0 C A:GLY140 4.0 28.0 1.0 CG1 A:VAL143 4.1 28.9 1.0 CB A:VAL143 4.2 27.8 1.0 SD A:MET202 4.3 30.9 1.0 CG A:MET202 4.3 29.1 1.0 N A:ASN139 4.4 19.8 1.0 CG2 A:VAL143 4.5 30.3 1.0 C8 A:TCL502 4.5 57.2 1.0 OD1 A:ASN139 4.5 33.4 1.0 O A:ASN139 4.6 21.5 1.0 C A:ALA138 4.9 24.2 1.0 CE A:MET202 4.9 21.5 1.0 O A:ALA138 5.0 22.4 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Brassica Napus Enoyl Acyl Carrier Protein Reductase Complexed with Nad and Triclosan


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Brassica Napus Enoyl Acyl Carrier Protein Reductase Complexed with Nad and Triclosan within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:34.0 occ:1.00 CL16 A:TCL502 0.0 34.0 1.0 C9 A:TCL502 1.7 45.4 1.0 C10 A:TCL502 2.7 19.8 1.0 C8 A:TCL502 2.8 57.2 1.0 O7 A:TCL502 3.0 28.7 1.0 O5D A:NAD501 3.4 33.5 1.0 C5B A:NAD501 3.6 34.8 1.0 O3 A:NAD501 3.6 62.4 1.0 O A:HOH569 3.7 54.5 1.0 C2D A:NAD501 3.8 22.0 1.0 C3D A:NAD501 3.9 18.2 1.0 CB A:ALA138 3.9 14.9 1.0 C11 A:TCL502 4.0 50.5 1.0 C13 A:TCL502 4.0 34.6 1.0 PN A:NAD501 4.1 31.7 1.0 O5B A:NAD501 4.1 50.9 1.0 O A:ALA138 4.2 22.4 1.0 O1N A:NAD501 4.2 40.5 1.0 C5 A:TCL502 4.3 33.7 1.0 O2D A:NAD501 4.3 22.4 1.0 O1A A:NAD501 4.3 76.4 1.0 PA A:NAD501 4.4 34.3 1.0 C5D A:NAD501 4.4 23.9 1.0 C12 A:TCL502 4.5 64.0 1.0 N A:ALA138 4.6 20.2 1.0 C A:ALA138 4.6 24.2 1.0 CA A:ALA138 4.6 15.8 1.0 O A:HOH570 4.7 42.1 1.0 C4D A:NAD501 4.7 21.5 1.0 C4 A:TCL502 4.9 26.2 1.0 C4B A:NAD501 4.9 37.6 1.0

A.Roujeinikova, C.W.Levy, S.Rowsell, S.Sedelnikova, P.J.Baker, C.A.Minshull, A.Mistry, J.G.Colls, R.Camble, A.R.Stuitje, A.R.Slabas, J.B.Rafferty, R.A.Pauptit, R.Viner, D.W.Rice. Crystallographic Analysis of Triclosan Bound to Enoyl Reductase. J.Mol.Biol. V. 294 527 1999.
ISSN: ISSN 0022-2836
PubMed: 10610777
DOI: 10.1006/JMBI.1999.3240