Zinc in PDB 8aut: WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C

The structure of WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C, PDB code: 8aut was solved by R.Buller, S.Hueppi, M.Voss, D.Schaub, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.17 / 2.69
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	106.458, 106.458, 385.22, 90, 90, 120
R / Rfree (%)	18.6 / 23.2

The structure of WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Zinc atom in the WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C (pdb code 8aut). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C, PDB code: 8aut:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:81.0 occ:1.00 HE2 A:HIS259 1.3 30.0 0.0 HE2 A:HIS164 1.3 30.0 0.0 O2 A:AKG303 2.0 123.8 1.0 NE2 A:HIS164 2.1 58.1 1.0 NE2 A:HIS259 2.1 66.0 1.0 O5 A:AKG303 2.3 77.5 1.0 CL A:CL302 2.4 97.2 1.0 C1 A:AKG303 2.8 130.6 1.0 C2 A:AKG303 2.8 95.2 1.0 CD2 A:HIS259 3.0 63.4 1.0 CE1 A:HIS164 3.0 58.7 1.0 HD2 A:HIS259 3.1 63.5 1.0 HE1 A:HIS164 3.1 58.7 1.0 CD2 A:HIS164 3.1 59.6 1.0 CE1 A:HIS259 3.2 65.8 1.0 HD2 A:HIS164 3.4 61.8 1.0 HE1 A:HIS259 3.4 67.7 1.0 H17 A:OAU304 3.6 99.9 1.0 O1 A:AKG303 4.0 164.3 1.0 HZ A:PHE252 4.1 68.2 1.0 ND1 A:HIS164 4.1 65.0 1.0 CG A:HIS259 4.1 64.5 1.0 OG A:SER189 4.2 74.0 1.0 ND1 A:HIS259 4.2 71.0 1.0 CG A:HIS164 4.2 67.8 1.0 C3 A:AKG303 4.3 100.3 1.0 HG A:SER189 4.4 30.0 0.0 HE2 A:PHE169 4.4 84.0 1.0 C17 A:OAU304 4.5 101.4 1.0 H16 A:OAU304 4.5 102.9 1.0 HE1 A:PHE276 4.6 88.1 1.0 HB3 A:SER189 4.6 70.8 1.0 H18 A:OAU304 4.6 100.0 1.0 H32 A:AKG303 4.6 97.1 1.0 H31 A:AKG303 4.8 96.6 1.0 HA3 A:GLY254 4.8 65.5 1.0 CB A:SER189 4.8 69.5 1.0 HD1 A:HIS164 4.9 30.0 0.0 C16 A:OAU304 4.9 103.9 1.0 H15 A:OAU304 4.9 103.8 1.0 CZ A:PHE252 4.9 68.6 1.0 HB2 A:SER189 5.0 70.8 1.0 HD1 A:HIS259 5.0 30.0 0.0 H42 A:AKG303 5.0 92.1 1.0

Zinc binding site 2 out of 4 in the WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:87.6 occ:1.00 HE2 B:HIS164 1.3 30.0 0.0 HE2 B:HIS259 1.4 30.0 0.0 O1 B:AKG303 2.0 110.9 1.0 NE2 B:HIS164 2.1 75.0 1.0 NE2 B:HIS259 2.2 76.7 1.0 CL B:CL302 2.4 129.8 1.0 O5 B:AKG303 2.5 95.0 1.0 C1 B:AKG303 2.8 106.7 1.0 C2 B:AKG303 3.0 99.7 1.0 CE1 B:HIS164 3.1 80.0 1.0 CD2 B:HIS164 3.1 73.4 1.0 CD2 B:HIS259 3.2 84.1 1.0 CE1 B:HIS259 3.2 76.5 1.0 HE1 B:HIS164 3.3 77.3 1.0 HD2 B:HIS259 3.3 81.5 1.0 HD2 B:HIS164 3.3 75.3 1.0 HE1 B:HIS259 3.4 78.7 1.0 H17 B:OAU304 3.7 120.9 1.0 O2 B:AKG303 4.0 100.5 1.0 OG B:SER189 4.1 76.7 1.0 HE2 B:PHE169 4.1 121.9 1.0 ND1 B:HIS164 4.2 79.3 1.0 CG B:HIS164 4.2 78.3 1.0 H16 B:OAU304 4.2 122.3 1.0 HE1 B:PHE276 4.2 95.3 1.0 HZ B:PHE252 4.3 84.7 1.0 HG B:SER189 4.3 30.0 0.0 ND1 B:HIS259 4.3 84.0 1.0 CG B:HIS259 4.3 84.0 1.0 H18 B:OAU304 4.3 121.8 1.0 C17 B:OAU304 4.4 123.6 1.0 C3 B:AKG303 4.5 99.2 1.0 HB3 B:SER189 4.6 72.0 1.0 C16 B:OAU304 4.8 123.8 1.0 H42 B:AKG303 4.8 93.8 1.0 HA3 B:GLY254 4.8 85.2 1.0 CB B:SER189 4.8 71.1 1.0 HZ B:PHE169 4.8 119.5 1.0 H15 B:OAU304 4.9 122.4 1.0 H32 B:AKG303 4.9 98.2 1.0 CE2 B:PHE169 4.9 123.1 1.0 H24 B:OAU304 4.9 90.0 1.0 H31 B:AKG303 5.0 97.1 1.0 HD1 B:HIS164 5.0 30.0 0.0

Zinc binding site 3 out of 4 in the WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn301 b:90.3 occ:1.00 HE2 C:HIS164 1.3 30.0 0.0 HE2 C:HIS259 1.4 30.0 0.0 O5 C:AKG303 2.1 91.1 1.0 O2 C:AKG303 2.1 118.5 1.0 NE2 C:HIS164 2.2 77.0 1.0 NE2 C:HIS259 2.3 82.8 1.0 CL C:CL302 2.5 112.5 1.0 C2 C:AKG303 2.8 100.2 1.0 C1 C:AKG303 2.9 115.3 1.0 CE1 C:HIS164 3.0 78.5 1.0 CD2 C:HIS259 3.1 87.3 1.0 CD2 C:HIS164 3.2 75.7 1.0 HE1 C:HIS164 3.2 77.2 1.0 HD2 C:HIS259 3.2 86.2 1.0 CE1 C:HIS259 3.3 94.4 1.0 HD2 C:HIS164 3.4 77.8 1.0 HE1 C:HIS259 3.5 92.8 1.0 H17 C:OAU304 3.6 113.2 1.0 O1 C:AKG303 4.1 127.4 1.0 ND1 C:HIS164 4.2 82.1 1.0 OG C:SER189 4.2 91.6 1.0 HZ C:PHE252 4.2 81.6 1.0 C3 C:AKG303 4.2 98.9 1.0 CG C:HIS164 4.2 80.4 1.0 HE2 C:PHE169 4.3 101.3 1.0 CG C:HIS259 4.3 91.0 1.0 H16 C:OAU304 4.3 114.0 1.0 H18 C:OAU304 4.3 113.3 1.0 ND1 C:HIS259 4.3 97.8 1.0 C17 C:OAU304 4.3 118.4 1.0 HE1 C:PHE276 4.4 103.6 1.0 HG C:SER189 4.4 30.0 0.0 HB3 C:SER189 4.5 86.0 1.0 H32 C:AKG303 4.5 100.2 1.0 C16 C:OAU304 4.8 113.2 1.0 H31 C:AKG303 4.8 99.2 1.0 H15 C:OAU304 4.8 114.4 1.0 CB C:SER189 4.8 85.8 1.0 H42 C:AKG303 4.8 100.2 1.0 H24 C:OAU304 4.9 99.7 1.0 HA3 C:GLY254 4.9 82.0 1.0 HD1 C:HIS164 4.9 30.0 0.0 HB2 C:SER189 5.0 86.4 1.0

Zinc binding site 4 out of 4 in the WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of WELO5* L221A Bound to Zn(II), Cl, 2-Oxoglutarate, and 12-Epi- Hapalindole C within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn301 b:81.0 occ:1.00 HE2 D:HIS164 1.2 30.0 0.0 HE2 D:HIS259 1.5 30.0 0.0 O1 D:AKG303 1.8 100.9 1.0 NE2 D:HIS164 2.0 65.8 1.0 NE2 D:HIS259 2.3 77.6 1.0 CL D:CL302 2.5 90.7 1.0 O5 D:AKG303 2.6 77.7 1.0 C1 D:AKG303 2.8 97.8 1.0 CE1 D:HIS164 2.9 63.2 1.0 C2 D:AKG303 3.0 85.1 1.0 HE1 D:HIS164 3.0 64.3 1.0 CD2 D:HIS164 3.1 71.2 1.0 CD2 D:HIS259 3.1 75.2 1.0 HD2 D:HIS259 3.2 75.0 1.0 CE1 D:HIS259 3.3 73.4 1.0 HD2 D:HIS164 3.3 71.1 1.0 HE1 D:HIS259 3.6 76.4 1.0 H17 D:OAU304 3.6 92.7 1.0 O2 D:AKG303 3.9 99.8 1.0 ND1 D:HIS164 4.0 72.2 1.0 CG D:HIS164 4.1 73.3 1.0 OG D:SER189 4.2 76.9 1.0 HZ D:PHE252 4.2 62.7 1.0 CG D:HIS259 4.2 76.4 1.0 H16 D:OAU304 4.3 96.1 1.0 H18 D:OAU304 4.3 92.5 1.0 HE2 D:PHE169 4.3 90.0 1.0 ND1 D:HIS259 4.3 78.7 1.0 C17 D:OAU304 4.4 95.5 1.0 HG D:SER189 4.4 30.0 0.0 C3 D:AKG303 4.5 86.9 1.0 HE1 D:PHE276 4.5 80.8 1.0 HB3 D:SER189 4.6 73.1 1.0 C16 D:OAU304 4.8 95.3 1.0 HD1 D:HIS164 4.8 30.0 0.0 H15 D:OAU304 4.9 97.2 1.0 H32 D:AKG303 4.9 85.7 1.0 CB D:SER189 4.9 72.2 1.0 H24 D:OAU304 4.9 89.5 1.0 H41 D:AKG303 4.9 85.0 1.0 HA3 D:GLY254 5.0 64.2 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