Zinc in PDB 5h82: Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form

The structure of Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form, PDB code: 5h82 was solved by A.Stavrinides, E.C.Tatsis, L.Caputi, E.Foureau, C.E.M.Stevenson, D.M.Lawson, V.Courdavault, S.E.O'connor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.69 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	72.360, 88.080, 121.390, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 22.5

The binding sites of Zinc atom in the Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form (pdb code 5h82). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form, PDB code: 5h82:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:28.3 occ:1.00 OE2 A:GLU71 1.9 24.1 1.0 NE2 A:HIS70 2.0 32.8 1.0 SG A:CYS48 2.3 31.8 1.0 SG A:CYS177 2.3 29.5 1.0 CE1 A:HIS70 3.0 29.6 1.0 CD A:GLU71 3.0 27.6 1.0 CD2 A:HIS70 3.0 30.8 1.0 CB A:CYS177 3.3 27.4 1.0 CB A:CYS48 3.4 34.1 1.0 CG A:GLU71 3.5 26.7 1.0 NH2 A:ARG205 3.5 39.3 1.0 ND1 A:HIS70 4.1 28.8 1.0 OE1 A:GLU71 4.1 27.2 1.0 CG A:HIS70 4.1 27.5 1.0 CZ A:ARG205 4.4 38.0 1.0 N A:CYS48 4.5 28.6 1.0 CA A:CYS48 4.5 32.4 1.0 NH1 A:ARG205 4.6 39.1 1.0 CA A:CYS177 4.7 28.6 1.0 O A:HOH1146 4.8 26.0 1.0 CB A:TRP50 4.8 30.7 1.0 C A:LEU47 4.9 29.6 1.0

Zinc binding site 2 out of 4 in the Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1002 b:37.9 occ:1.00 SG A:CYS101 2.3 42.4 1.0 SG A:CYS107 2.3 35.5 1.0 SG A:CYS115 2.3 38.2 1.0 SG A:CYS104 2.3 41.9 1.0 CB A:CYS115 3.3 37.0 1.0 CB A:CYS104 3.3 45.4 1.0 CB A:CYS101 3.4 43.7 1.0 CB A:CYS107 3.4 37.6 1.0 N A:CYS101 3.7 36.0 1.0 N A:CYS104 3.8 48.8 1.0 N A:GLY102 3.9 41.0 1.0 CA A:CYS101 4.0 41.0 1.0 CA A:CYS115 4.1 35.6 1.0 CA A:CYS104 4.1 45.8 1.0 N A:CYS107 4.2 34.7 1.0 C A:CYS101 4.3 42.7 1.0 CA A:CYS107 4.4 36.5 1.0 N A:LYS103 4.5 49.8 1.0 CD A:PRO116 4.5 41.5 1.0 CB A:SER100 4.6 33.6 1.0 C A:SER100 4.8 37.9 1.0 C A:CYS104 4.8 43.0 1.0 OG A:SER100 4.8 34.6 1.0 C A:CYS115 4.9 38.7 1.0 CA A:GLY102 4.9 44.0 1.0 C A:LYS103 4.9 52.0 1.0 N A:PRO116 4.9 38.6 1.0

Zinc binding site 3 out of 4 in the Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:30.3 occ:1.00 OE2 B:GLU71 1.9 31.2 1.0 NE2 B:HIS70 2.0 32.2 1.0 SG B:CYS48 2.3 30.2 1.0 SG B:CYS177 2.3 30.9 1.0 CE1 B:HIS70 2.9 34.8 1.0 CD B:GLU71 3.0 28.8 1.0 CD2 B:HIS70 3.0 35.0 1.0 CB B:CYS177 3.2 30.6 1.0 CB B:CYS48 3.4 31.6 1.0 CG B:GLU71 3.5 27.8 1.0 NH2 B:ARG205 3.5 40.5 1.0 ND1 B:HIS70 4.0 31.6 1.0 OE1 B:GLU71 4.1 26.6 1.0 CG B:HIS70 4.1 31.5 1.0 CZ B:ARG205 4.3 38.4 1.0 N B:CYS48 4.5 30.4 1.0 CA B:CYS48 4.5 31.1 1.0 NH1 B:ARG205 4.6 37.3 1.0 CA B:CYS177 4.7 30.8 1.0 O B:HOH1148 4.8 26.2 1.0 CB B:TRP50 4.8 33.6 1.0 C B:LEU47 4.8 30.8 1.0 CB B:GLU71 5.0 26.9 1.0

Zinc binding site 4 out of 4 in the Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Heteroyohimbine Synthase THAS2 From Catharanthus Roseus - Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1002 b:62.3 occ:1.00 SG B:CYS107 2.3 65.5 1.0 SG B:CYS115 2.3 80.0 1.0 SG B:CYS101 2.3 96.0 1.0 SG B:CYS104 2.4 75.6 1.0 CB B:CYS115 3.3 69.1 1.0 CB B:CYS104 3.4 83.5 1.0 CB B:CYS101 3.4 87.8 1.0 CB B:CYS107 3.4 74.6 1.0 N B:CYS101 3.7 75.9 1.0 N B:CYS104 3.8 83.9 1.0 N B:GLY102 3.9 82.9 1.0 CA B:CYS101 4.0 82.6 1.0 CA B:CYS115 4.0 65.6 1.0 CA B:CYS104 4.2 85.2 1.0 N B:CYS107 4.2 69.6 1.0 C B:CYS101 4.3 83.3 1.0 CA B:CYS107 4.4 74.1 1.0 CD B:PRO116 4.5 77.4 1.0 N B:LYS103 4.5 95.6 1.0 CB B:SER100 4.6 63.2 1.0 C B:SER100 4.8 69.8 1.0 OG B:SER100 4.8 65.8 1.0 C B:CYS104 4.9 82.1 1.0 C B:CYS115 4.9 67.6 1.0 N B:PRO116 4.9 75.7 1.0 CA B:GLY102 4.9 85.1 1.0 C B:LYS103 5.0 0.0 1.0

A.Stavrinides, E.C.Tatsis, L.Caputi, E.Foureau, C.E.Stevenson, D.M.Lawson, V.Courdavault, S.E.O'connor. Structural Investigation of Heteroyohimbine Alkaloid Synthesis Reveals Active Site Elements That Control Stereoselectivity. Nat Commun V. 7 12116 2016.
ISSN: ESSN 2041-1723
PubMed: 27418042
DOI: 10.1038/NCOMMS12116