Zinc in PDB 8acv: WELO5* Bound to Zn(II), Cl, and 2-Oxoglutarate

The structure of WELO5* Bound to Zn(II), Cl, and 2-Oxoglutarate, PDB code: 8acv was solved by R.Buller, S.Hueppi, M.Voss, T.Hayashi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.77 / 2.26
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	45.321, 83.097, 144.318, 90, 96.73, 90
R / Rfree (%)	19.5 / 23.6

The structure of WELO5* Bound to Zn(II), Cl, and 2-Oxoglutarate also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the WELO5* Bound to Zn(II), Cl, and 2-Oxoglutarate (pdb code 8acv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the WELO5* Bound to Zn(II), Cl, and 2-Oxoglutarate, PDB code: 8acv:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the WELO5* Bound to Zn(II), Cl, and 2-Oxoglutarate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of WELO5* Bound to Zn(II), Cl, and 2-Oxoglutarate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:60.3 occ:1.00 O2 A:AKG301 1.9 70.1 1.0 NE2 A:HIS259 1.9 57.8 1.0 NE2 A:HIS164 2.1 52.8 1.0 CL A:CL302 2.4 66.9 1.0 O5 A:AKG301 2.5 66.0 1.0 C1 A:AKG301 2.7 70.9 1.0 CD2 A:HIS259 2.9 58.1 1.0 CE1 A:HIS259 2.9 57.3 1.0 C2 A:AKG301 3.0 66.4 1.0 CD2 A:HIS164 3.1 53.4 1.0 CE1 A:HIS164 3.1 52.7 1.0 O1 A:AKG301 3.9 74.7 1.0 CG A:HIS259 4.0 56.4 1.0 ND1 A:HIS259 4.1 58.0 1.0 CG A:HIS164 4.2 52.5 1.0 ND1 A:HIS164 4.2 53.7 1.0 O1 A:GOL304 4.2 87.8 1.0 OG A:SER189 4.3 53.4 0.5 OG A:SER189 4.3 55.2 0.5 C3 A:AKG301 4.5 64.7 1.0 C1 A:GOL304 4.8 88.2 1.0 CZ A:PHE252 4.8 55.9 1.0 CE2 A:PHE169 5.0 76.8 1.0 CB A:SER189 5.0 51.5 0.5 CE1 A:PHE276 5.0 59.7 1.0

Zinc binding site 2 out of 2 in the WELO5* Bound to Zn(II), Cl, and 2-Oxoglutarate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of WELO5* Bound to Zn(II), Cl, and 2-Oxoglutarate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn304 b:74.7 occ:1.00 O1 B:AKG301 1.9 85.2 1.0 NE2 B:HIS164 2.0 79.3 1.0 NE2 B:HIS259 2.0 74.4 1.0 CL B:CL303 2.5 93.3 1.0 O5 B:AKG301 2.7 85.0 1.0 C1 B:AKG301 2.8 85.6 1.0 CE1 B:HIS259 2.9 74.2 1.0 CE1 B:HIS164 3.0 78.9 1.0 CD2 B:HIS164 3.0 79.6 1.0 CD2 B:HIS259 3.1 74.6 1.0 C2 B:AKG301 3.1 84.5 1.0 O2 B:AKG301 4.0 87.0 1.0 O B:HOH427 4.0 73.4 1.0 ND1 B:HIS259 4.1 74.8 1.0 ND1 B:HIS164 4.1 79.4 1.0 CG B:HIS164 4.1 77.9 1.0 CG B:HIS259 4.2 72.9 1.0 OG B:SER189 4.2 88.1 1.0 C3 B:AKG301 4.6 83.9 1.0 CE1 B:PHE276 4.7 89.5 1.0 CB B:SER189 4.9 78.7 1.0 CZ B:PHE252 4.9 80.2 1.0 CE2 B:PHE169 4.9 101.5 1.0

M.Voss, S.Huppi, D.Schaub, T.Hayashi, M.Ligibel, E.Sager, K.Schroer, R.Snajdrova, R.M.U.Buller. Enzyme Engineering Enables Inversion of Substrate Stereopreference of the Halogenase WELO5* Chemcatchem 2022.
ISSN: ESSN 1867-3899
DOI: 10.1002/CCTC.202201115