Chlorine in PDB 7ayc: Crystal Structure of Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q

All present enzymatic activity of Crystal Structure of Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q:
1.3.1.104;

The structure of Crystal Structure of Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q, PDB code: 7ayc was solved by M.T.Rahman, M.K.Koski, K.J.Autio, A.J.Kastaniotis, R.K.Wierenga, J.K.Hiltunen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.95 / 2.02
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	71.516, 71.516, 143.768, 90, 90, 120
R / Rfree (%)	21.8 / 25.3

The binding sites of Chlorine atom in the Crystal Structure of Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q (pdb code 7ayc). 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 Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q, PDB code: 7ayc:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q


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 Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:79.1 occ:0.50 CD A:LYS306 3.8 75.0 1.0 NH1 A:ARG308 3.9 61.9 1.0 CD A:ARG308 4.0 54.6 1.0 O A:HOH528 4.2 64.9 1.0 CB A:LYS306 4.3 55.6 1.0 CG A:LYS306 4.5 62.9 1.0 CG A:ARG308 4.7 50.4 1.0 CZ A:ARG308 4.8 63.8 1.0 NE A:ARG308 4.8 57.4 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q


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 Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:59.3 occ:1.00 O A:HOH508 3.3 65.5 1.0 N A:VAL236 3.3 55.8 1.0 NZ A:LYS229 3.4 75.4 1.0 CD2 A:HIS235 3.5 65.1 1.0 CA A:HIS235 3.6 57.1 1.0 O A:VAL236 3.6 56.2 1.0 CE A:LYS229 3.6 66.2 1.0 CB A:HIS235 3.7 56.3 1.0 CG A:HIS235 3.9 64.9 1.0 C A:HIS235 4.0 56.5 1.0 C A:VAL236 4.3 54.6 1.0 CA A:VAL236 4.3 56.9 1.0 O A:GLU234 4.4 62.0 1.0 NE2 A:HIS235 4.7 65.1 1.0 CZ A:PHE251 4.7 89.9 1.0 N A:HIS235 4.8 57.3 1.0 CE1 A:PHE251 4.8 91.6 1.0 CB A:VAL236 4.8 56.9 1.0 OG A:SER225 5.0 71.9 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q


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 Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:66.8 occ:1.00 OE2 A:GLU239 3.0 56.5 1.0 N A:ALA191 3.1 49.7 1.0 CA A:ALA191 3.6 50.9 1.0 N A:ARG216 3.6 59.6 1.0 C A:VAL215 3.7 58.5 1.0 CA A:VAL215 3.7 52.5 1.0 CD A:GLU239 3.9 62.3 1.0 CG A:GLU239 3.9 63.5 1.0 O A:HOH514 3.9 73.2 1.0 O A:VAL214 3.9 45.1 1.0 CB A:ASN190 4.0 49.3 1.0 CG2 A:VAL264 4.0 58.8 1.0 C A:ASN190 4.2 51.6 1.0 N A:VAL215 4.2 49.5 1.0 C A:VAL214 4.2 49.0 1.0 O A:VAL215 4.2 56.1 1.0 CA A:ASN190 4.4 47.0 1.0 CA A:ARG216 4.4 62.9 1.0 CB A:ALA191 4.4 57.1 1.0 CG1 A:VAL214 4.4 50.5 1.0 CB A:ARG216 4.5 74.2 1.0 O A:HOH544 4.8 69.0 1.0 CG A:ASN190 4.8 50.9 1.0 C A:ALA191 4.8 59.2 1.0 CB A:VAL214 4.9 48.9 1.0 N A:SER192 5.0 51.9 1.0

M.T.Rahman, M.K.Koski, K.J.Autio, A.J.Kastaniotis, R.K.Wierenga, J.K.Hiltunen. Crystal Structure of Human Mitochondrial 2-Enoyl Thioester Reductase (Mecr) with Single Mutation G165Q To Be Published.