Chlorine in PDB 3uzw: Crystal Structure of 5BETA-Reductase (AKR1D1) E120H Mutant in Complex with Nadp+

All present enzymatic activity of Crystal Structure of 5BETA-Reductase (AKR1D1) E120H Mutant in Complex with Nadp+:
1.3.1.3;

The structure of Crystal Structure of 5BETA-Reductase (AKR1D1) E120H Mutant in Complex with Nadp+, PDB code: 3uzw was solved by M.Chen, D.W.Christianson, T.M.Penning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.29 / 1.89
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.134, 110.127, 129.394, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 21.1

The binding sites of Chlorine atom in the Crystal Structure of 5BETA-Reductase (AKR1D1) E120H Mutant in Complex with Nadp+ (pdb code 3uzw). 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 5BETA-Reductase (AKR1D1) E120H Mutant in Complex with Nadp+, PDB code: 3uzw:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of 5BETA-Reductase (AKR1D1) E120H Mutant in Complex with Nadp+


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 5BETA-Reductase (AKR1D1) E120H Mutant in Complex with Nadp+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl601 b:19.0 occ:1.00 O A:HOH1011 3.0 17.1 1.0 O A:HOH1043 3.0 18.3 1.0 N A:TRP89 3.3 14.1 1.0 O A:HOH1009 3.3 10.9 1.0 NH2 A:ARG104 3.5 11.7 1.0 CB A:TRP89 3.6 14.4 1.0 O A:LYS87 3.7 8.0 1.0 CG2 A:THR101 3.7 13.2 1.0 O A:HOH1119 4.0 19.5 1.0 CA A:TRP89 4.1 14.7 1.0 O A:HOH1003 4.2 11.8 1.0 CA A:LEU88 4.2 10.6 1.0 CG2 A:ILE57 4.2 15.5 1.0 C A:LEU88 4.2 11.7 1.0 CG A:ASN92 4.3 19.3 1.0 CB A:TYR56 4.3 13.8 1.0 OD1 A:ASN92 4.3 30.8 1.0 ND2 A:ASN92 4.5 21.3 1.0 C A:LYS87 4.7 8.6 1.0 CD2 A:TYR56 4.7 16.2 1.0 CB A:ASN92 4.7 16.2 1.0 CZ A:ARG104 4.8 16.6 1.0 OH A:TYR117 4.9 10.6 1.0 N A:LEU88 4.9 8.9 1.0 CG A:TYR56 4.9 13.5 1.0 CG A:TRP89 5.0 17.5 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of 5BETA-Reductase (AKR1D1) E120H Mutant in Complex with Nadp+


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 5BETA-Reductase (AKR1D1) E120H Mutant in Complex with Nadp+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl601 b:13.8 occ:1.00 O B:HOH1012 3.1 12.1 1.0 O B:HOH1174 3.2 19.9 1.0 O B:HOH1065 3.2 9.0 1.0 N B:TRP89 3.2 8.3 1.0 NH2 B:ARG104 3.3 12.2 1.0 ND2 B:ASN92 3.4 16.4 1.0 CG2 B:THR101 3.5 12.1 1.0 CB B:TRP89 3.6 9.7 1.0 O B:LYS87 3.6 10.3 1.0 CA B:TRP89 4.0 7.4 1.0 O B:HOH1010 4.1 10.9 1.0 C B:LEU88 4.2 9.2 1.0 CA B:LEU88 4.2 9.5 1.0 O B:HOH1062 4.2 15.3 1.0 CG2 B:ILE57 4.4 10.9 1.0 CB B:TYR56 4.4 8.5 1.0 CG B:ASN92 4.5 16.4 1.0 CZ B:ARG104 4.6 11.3 1.0 C B:LYS87 4.7 9.7 1.0 OH B:TYR117 4.7 12.5 1.0 CB B:ASN92 4.9 9.8 1.0 CD2 B:TYR56 4.9 11.8 1.0 N B:LEU88 4.9 8.3 1.0 CG B:TRP89 5.0 9.5 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of 5BETA-Reductase (AKR1D1) E120H Mutant in Complex with Nadp+


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 5BETA-Reductase (AKR1D1) E120H Mutant in Complex with Nadp+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl602 b:20.4 occ:1.00 OG1 B:THR292 3.1 10.6 1.0 O B:HOH1166 3.5 21.9 1.0 CG2 B:THR292 3.9 10.8 1.0 CB B:THR292 3.9 12.8 1.0 OE1 B:GLU294 3.9 17.0 1.0 CB B:GLU294 3.9 14.3 1.0 CG B:GLU295 4.2 10.6 1.0 CD B:GLU295 4.3 9.8 1.0 OE2 B:GLU295 4.3 9.6 1.0 CD B:GLU294 4.4 26.1 1.0 NH1 B:ARG250 4.4 9.9 1.0 CG B:GLU294 4.6 21.3 1.0 N B:GLU295 4.7 8.2 1.0 OE1 B:GLU295 4.9 11.4 1.0 CA B:GLU294 5.0 11.5 1.0

M.Chen, J.E.Drury, D.W.Christianson, T.M.Penning. Conversion of Human Steroid 5BETA-Reductase (AKR1D1) Into 3β-Hydroxysteroid Dehydrogenase By Single Point Mutation E120H: Example of Perfect Enzyme Engineering. J.Biol.Chem. V. 287 16609 2012.
ISSN: ISSN 0021-9258
PubMed: 22437839
DOI: 10.1074/JBC.M111.338780