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Zinc in PDB 8t1t: Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona with Qsy Deletion) Heteromeric Complex (Bound to Sam)

Protein crystallography data

The structure of Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona with Qsy Deletion) Heteromeric Complex (Bound to Sam), PDB code: 8t1t was solved by K.K.Crone, T.Jomori, F.S.Miller, J.Gralnick, M.Elias, M.F.Freeman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.13 / 1.55
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 52.5, 59.3, 60.1, 95.9, 96.5, 112.6
R / Rfree (%) 17.3 / 20.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona with Qsy Deletion) Heteromeric Complex (Bound to Sam) (pdb code 8t1t). 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 Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona with Qsy Deletion) Heteromeric Complex (Bound to Sam), PDB code: 8t1t:

Zinc binding site 1 out of 1 in 8t1t

Go back to Zinc Binding Sites List in 8t1t
Zinc binding site 1 out of 1 in the Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona with Qsy Deletion) Heteromeric Complex (Bound to Sam)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona with Qsy Deletion) Heteromeric Complex (Bound to Sam) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn302

b:16.9
occ:0.40
OE2 C:GLU126 1.9 37.6 1.0
NE2 C:HIS142 2.1 30.1 0.7
NE2 A:HIS142 2.1 29.5 1.0
OE2 A:GLU126 2.2 50.6 1.0
NE2 C:HIS142 2.3 17.8 0.3
CE1 C:HIS142 2.5 29.6 0.7
CD C:GLU126 2.7 29.6 1.0
CD A:GLU126 2.9 38.0 1.0
OE1 C:GLU126 3.0 34.4 1.0
OE1 A:GLU126 3.0 33.6 1.0
CE1 A:HIS142 3.1 26.4 1.0
CD2 A:HIS142 3.2 23.9 1.0
CE1 C:HIS142 3.2 15.6 0.3
CD2 C:HIS142 3.2 16.4 0.3
CD2 C:HIS142 3.3 37.1 0.7
ND1 C:HIS142 3.8 37.4 0.7
O C:HOH557 3.9 42.5 1.0
O A:HOH509 3.9 47.1 1.0
O C:HOH547 4.0 44.6 1.0
CG C:GLU126 4.2 22.2 1.0
CG C:HIS142 4.2 26.5 0.7
ND1 A:HIS142 4.2 25.5 1.0
ND1 C:HIS142 4.3 17.5 0.3
CG A:HIS142 4.3 21.3 1.0
CG C:HIS142 4.3 16.4 0.3
CG A:GLU126 4.4 32.9 1.0
OG C:SER144 4.7 19.1 0.5
O C:HOH465 4.8 38.6 1.0
OG A:SER144 4.8 20.5 1.0
NE1 C:TRP130 5.0 21.6 1.0
CZ2 C:TRP130 5.0 20.1 1.0

Reference:

K.K.Crone, T.Jomori, F.S.Miller, J.A.Gralnick, M.H.Elias, M.F.Freeman. Ripp Enzyme Heterocomplex Structure-Guided Discovery of A Bacterial Borosin Alpha- N -Methylated Peptide Natural Product. Rsc Chem Biol V. 4 804 2023.
ISSN: ESSN 2633-0679
PubMed: 37799586
DOI: 10.1039/D3CB00093A
Page generated: Thu Dec 28 13:40:48 2023

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