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Arsenic in PDB 8d59: Crystal Structure of Human METTL1 in Complex with Sam

Enzymatic activity of Crystal Structure of Human METTL1 in Complex with Sam

All present enzymatic activity of Crystal Structure of Human METTL1 in Complex with Sam:
2.1.1.33;

Protein crystallography data

The structure of Crystal Structure of Human METTL1 in Complex with Sam, PDB code: 8d59 was solved by R.Raj, K.Babu, Y.Nam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.25 / 2.26
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 86.026, 86.026, 65.579, 90, 90, 120
R / Rfree (%) 20.7 / 23

Other elements in 8d59:

The structure of Crystal Structure of Human METTL1 in Complex with Sam also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Human METTL1 in Complex with Sam (pdb code 8d59). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Crystal Structure of Human METTL1 in Complex with Sam, PDB code: 8d59:

Arsenic binding site 1 out of 1 in 8d59

Go back to Arsenic Binding Sites List in 8d59
Arsenic binding site 1 out of 1 in the Crystal Structure of Human METTL1 in Complex with Sam


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Human METTL1 in Complex with Sam within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As304

b:130.6
occ:1.00
AS A:CAC304 0.0 130.6 1.0
O2 A:CAC304 1.7 82.0 1.0
O1 A:CAC304 1.7 96.3 1.0
C2 A:CAC304 2.0 74.4 1.0
C1 A:CAC304 2.0 86.2 1.0
NH2 A:ARG246 3.7 54.7 1.0
ND2 A:ASN247 4.0 65.6 1.0
CG A:LYS243 4.3 55.8 1.0
CE A:LYS243 4.4 63.5 1.0
NE A:ARG246 4.4 58.5 1.0
CZ A:ARG246 4.6 59.2 1.0
CD A:LYS243 4.7 62.0 1.0
OD1 A:ASN247 4.8 87.1 1.0
CG A:ASN247 4.9 63.6 1.0

Reference:

V.M.Ruiz-Arroyo, R.Raj, K.Babu, O.Onolbaatar, P.H.Roberts, Y.Nam. Structures and Mechanisms of Trna Methylation By METTL1-WDR4. Nature 2023.
ISSN: ESSN 1476-4687
PubMed: 36599982
DOI: 10.1038/S41586-022-05565-5
Page generated: Wed Jul 10 13:58:55 2024

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