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Zinc in PDB 8ftr: Sgvm Methyltransferase with Mta and Alpha-Ketoleucine

Protein crystallography data

The structure of Sgvm Methyltransferase with Mta and Alpha-Ketoleucine, PDB code: 8ftr was solved by K.Kuzelka, S.K.Nair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 54.27 / 2.13
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 67.134, 67.134, 184.338, 90, 90, 90
R / Rfree (%) 21.1 / 24.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Sgvm Methyltransferase with Mta and Alpha-Ketoleucine (pdb code 8ftr). 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 Sgvm Methyltransferase with Mta and Alpha-Ketoleucine, PDB code: 8ftr:

Zinc binding site 1 out of 1 in 8ftr

Go back to Zinc Binding Sites List in 8ftr
Zinc binding site 1 out of 1 in the Sgvm Methyltransferase with Mta and Alpha-Ketoleucine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Sgvm Methyltransferase with Mta and Alpha-Ketoleucine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:68.7
occ:1.00
NE2 A:HIS296 2.3 51.2 1.0
NE2 A:HIS244 2.3 57.5 1.0
O3 A:COI502 2.6 54.9 1.0
O2 A:COI502 2.7 56.5 1.0
O A:HOH611 2.9 59.8 1.0
CE1 A:HIS244 3.0 54.8 1.0
CD2 A:HIS296 3.2 46.5 1.0
C2 A:COI502 3.3 50.8 1.0
C1 A:COI502 3.3 46.3 1.0
CE1 A:HIS296 3.4 43.9 1.0
OD2 A:ASP245 3.4 67.4 1.0
CD2 A:HIS244 3.5 54.4 1.0
OD1 A:ASP245 3.7 64.2 1.0
CG A:ASP245 4.0 66.1 1.0
ND1 A:HIS244 4.2 53.1 1.0
CE A:MET300 4.4 46.6 1.0
CG A:HIS296 4.4 46.1 1.0
ND1 A:HIS296 4.4 42.9 1.0
O1 A:COI502 4.5 41.7 1.0
SD A:MET300 4.5 52.1 1.0
CG A:HIS244 4.5 55.3 1.0
O A:PHE241 4.6 54.7 1.0
C3 A:COI502 4.7 47.6 1.0
NH2 A:ARG132 4.8 39.2 1.0

Reference:

S.Ju, K.P.Kuzelka, R.Guo, B.Krohn-Hansen, J.Wu, S.K.Nair, Y.Yang. A Biocatalytic Platform For Asymmetric Alkylation of Alpha-Keto Acids By Mining and Engineering of Methyltransferases. Nat Commun V. 14 5704 2023.
ISSN: ESSN 2041-1723
PubMed: 37709735
DOI: 10.1038/S41467-023-40980-W
Page generated: Thu Dec 28 13:03:01 2023

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