Zinc in PDB 8rww: Crystal Structure of Native Alpha-Keto C-Methyl Transferase Sgvm Bound to Ketoleucine

The structure of Crystal Structure of Native Alpha-Keto C-Methyl Transferase Sgvm Bound to Ketoleucine, PDB code: 8rww was solved by S.Gerhardt, J.N.Andexer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.09 / 1.95
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	67.278, 67.278, 182.967, 90, 90, 90
R / Rfree (%)	18.2 / 21.2

The structure of Crystal Structure of Native Alpha-Keto C-Methyl Transferase Sgvm Bound to Ketoleucine also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Native Alpha-Keto C-Methyl Transferase Sgvm Bound to Ketoleucine (pdb code 8rww). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Native Alpha-Keto C-Methyl Transferase Sgvm Bound to Ketoleucine, PDB code: 8rww:

Zinc binding site 1 out of 1 in the Crystal Structure of Native Alpha-Keto C-Methyl Transferase Sgvm Bound to Ketoleucine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Native Alpha-Keto C-Methyl Transferase Sgvm Bound to Ketoleucine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:43.2 occ:1.00 O3 A:COI1002 2.0 48.4 1.0 NE2 A:HIS296 2.2 33.0 1.0 O A:HOH1256 2.2 48.4 1.0 NE2 A:HIS244 2.2 42.9 1.0 O1 A:COI1002 2.4 47.7 1.0 O A:HOH1261 2.5 52.7 1.0 C2 A:COI1002 2.8 49.0 1.0 C1 A:COI1002 3.0 47.0 1.0 CD2 A:HIS296 3.1 33.3 1.0 CE1 A:HIS244 3.1 43.0 1.0 CE1 A:HIS296 3.2 33.3 1.0 HE1 A:HIS244 3.2 43.0 1.0 HD2 A:HIS296 3.3 33.3 1.0 CD2 A:HIS244 3.3 42.3 1.0 HE1 A:HIS296 3.5 33.3 1.0 HD2 A:HIS244 3.6 42.3 1.0 OD1 A:ASP245 4.0 65.9 1.0 O A:HOH1172 4.0 79.2 1.0 HE3 A:MET300 4.0 36.6 1.0 HE1 A:MET300 4.0 36.6 1.0 HH22 A:ARG132 4.2 35.6 1.0 O2 A:COI1002 4.2 45.8 1.0 C3 A:COI1002 4.2 50.3 1.0 H53 A:COI1002 4.2 50.6 1.0 CG A:HIS296 4.3 33.2 1.0 ND1 A:HIS244 4.3 42.8 1.0 ND1 A:HIS296 4.3 33.9 1.0 CG A:HIS244 4.4 41.9 1.0 CE A:MET300 4.5 36.6 1.0 H31 A:COI1002 4.6 50.3 1.0 H4 A:COI1002 4.6 50.4 1.0 HB3 A:PHE241 4.7 43.9 1.0 HZ2 A:TRP104 4.7 27.9 1.0 HD21 A:LEU304 4.8 37.9 1.0 C4 A:COI1002 4.9 50.4 1.0 O A:HOH1297 4.9 83.0 1.0 H32 A:COI1002 4.9 50.3 1.0 CG A:ASP245 5.0 65.2 1.0

C.Sommer-Kamann, J.Breiltgens, Z.Zou, S.Gerhardt, R.Saleem-Batcha, F.Kemper, O.Einsle, J.N.Andexer, M.Muller. Structures and Protein Engineering of the Alpha-Keto Acid C-Methyltransferases Sgvm and Mrsa For Rational Substrate Transfer. Chembiochem 00258 2024.
ISSN: ESSN 1439-7633
PubMed: 38887142
DOI: 10.1002/CBIC.202400258