Chlorine in PDB 2std: Scytalone Dehydratase Complexed with Tight-Binding Inhibitor Carpropamid

All present enzymatic activity of Scytalone Dehydratase Complexed with Tight-Binding Inhibitor Carpropamid:
4.2.1.94;

The structure of Scytalone Dehydratase Complexed with Tight-Binding Inhibitor Carpropamid, PDB code: 2std was solved by M.Nakasako, T.Motoyama, Y.Kurahashi, I.Yamaguchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.10
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	74.540, 74.540, 71.200, 90.00, 90.00, 120.00
R / Rfree (%)	17.9 / 25.9

The binding sites of Chlorine atom in the Scytalone Dehydratase Complexed with Tight-Binding Inhibitor Carpropamid (pdb code 2std). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Scytalone Dehydratase Complexed with Tight-Binding Inhibitor Carpropamid, PDB code: 2std:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Scytalone Dehydratase Complexed with Tight-Binding Inhibitor Carpropamid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Scytalone Dehydratase Complexed with Tight-Binding Inhibitor Carpropamid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl175 b:10.7 occ:1.00 CL0 A:CRP175 0.0 10.7 1.0 C4' A:CRP175 1.9 26.9 1.0 C5' A:CRP175 2.8 23.2 1.0 C3' A:CRP175 2.8 26.4 1.0 CZ A:PHE158 3.6 43.7 1.0 CA A:GLY165 3.9 41.3 1.0 CD2 A:PHE169 3.9 44.1 1.0 CE1 A:PHE158 4.0 43.6 1.0 CG2 A:VAL75 4.1 25.1 1.0 O A:GLY165 4.1 41.6 1.0 C6' A:CRP175 4.1 24.9 1.0 CD1 A:LEU54 4.1 47.0 1.0 C A:GLY165 4.1 42.0 1.0 C2' A:CRP175 4.1 25.3 1.0 CB A:PHE169 4.6 46.9 1.0 CG A:PHE169 4.6 45.2 1.0 CE2 A:PHE169 4.6 39.3 1.0 C1' A:CRP175 4.6 25.6 1.0 CE2 A:PHE158 4.8 44.1 1.0 SD A:MET69 5.0 32.7 1.0 CG A:MET69 5.0 31.2 1.0

Chlorine binding site 2 out of 3 in the Scytalone Dehydratase Complexed with Tight-Binding Inhibitor Carpropamid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Scytalone Dehydratase Complexed with Tight-Binding Inhibitor Carpropamid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl175 b:10.0 occ:1.00 CL1 A:CRP175 0.0 10.0 1.0 C2 A:CRP175 1.8 18.5 1.0 C1 A:CRP175 2.8 21.0 1.0 C3 A:CRP175 2.8 18.7 1.0 CL2 A:CRP175 2.9 9.1 1.0 C A:CRP175 3.1 26.1 1.0 O A:CRP175 3.3 27.6 1.0 CH2 A:TRP26 3.5 19.2 1.0 CZ2 A:TRP26 3.6 19.7 1.0 CD2 A:HIS85 3.9 21.5 1.0 N A:CRP175 3.9 27.9 1.0 CD2 A:LEU147 3.9 18.6 1.0 CD1 A:LEU106 4.0 28.4 1.0 C5 A:CRP175 4.1 24.8 1.0 C4 A:CRP175 4.1 22.5 1.0 OD1 A:ASN131 4.3 28.8 1.0 O A:HOH275 4.4 23.0 1.0 NE2 A:HIS85 4.4 23.9 1.0 CE2 A:TYR30 4.4 17.8 1.0 C7' A:CRP175 4.9 25.6 1.0 CZ3 A:TRP26 4.9 17.7 1.0 ND2 A:ASN131 4.9 19.5 1.0 CE2 A:TRP26 4.9 19.8 1.0 CG A:ASN131 5.0 22.1 1.0

Chlorine binding site 3 out of 3 in the Scytalone Dehydratase Complexed with Tight-Binding Inhibitor Carpropamid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Scytalone Dehydratase Complexed with Tight-Binding Inhibitor Carpropamid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl175 b:9.1 occ:1.00 CL2 A:CRP175 0.0 9.1 1.0 C2 A:CRP175 1.8 18.5 1.0 C3 A:CRP175 2.8 18.7 1.0 C1 A:CRP175 2.8 21.0 1.0 CL1 A:CRP175 2.9 10.0 1.0 C4 A:CRP175 3.1 22.5 1.0 C5 A:CRP175 3.1 24.8 1.0 ND2 A:ASN131 3.4 19.5 1.0 CB A:PRO149 3.9 26.0 1.0 OG A:SER129 3.9 23.7 1.0 C A:CRP175 4.1 26.1 1.0 CD1 A:LEU106 4.1 28.4 1.0 CG A:PRO149 4.1 27.2 1.0 OD1 A:ASN131 4.2 28.8 1.0 CG A:ASN131 4.2 22.1 1.0 CB A:SER129 4.2 23.0 1.0 CD1 A:ILE151 4.2 31.4 1.0 CG1 A:ILE151 4.4 33.1 1.0 O A:CRP175 4.4 27.6 1.0 C6 A:CRP175 4.5 25.9 1.0 CD2 A:LEU147 4.9 18.6 1.0 CA A:PRO149 4.9 23.9 1.0

M.Nakasako, T.Motoyama, Y.Kurahashi, I.Yamaguchi. Cryogenic X-Ray Crystal Structure Analysis For the Complex of Scytalone Dehydratase of A Rice Blast Fungus and Its Tight-Binding Inhibitor, Carpropamid: the Structural Basis of Tight-Binding Inhibition. Biochemistry V. 37 9931 1998.
ISSN: ISSN 0006-2960
PubMed: 9665698
DOI: 10.1021/BI980321B