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Calcium in PDB 5yf0: Crystal Structure of CARNMT1 Bound to Sam

Enzymatic activity of Crystal Structure of CARNMT1 Bound to Sam

All present enzymatic activity of Crystal Structure of CARNMT1 Bound to Sam:
2.1.1.22;

Protein crystallography data

The structure of Crystal Structure of CARNMT1 Bound to Sam, PDB code: 5yf0 was solved by R.Cao, X.Zhang, H.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.56 / 2.25
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 127.769, 127.769, 324.957, 90.00, 90.00, 120.00
R / Rfree (%) 17.1 / 19.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of CARNMT1 Bound to Sam (pdb code 5yf0). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of CARNMT1 Bound to Sam, PDB code: 5yf0:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 5yf0

Go back to Calcium Binding Sites List in 5yf0
Calcium binding site 1 out of 2 in the Crystal Structure of CARNMT1 Bound to Sam


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of CARNMT1 Bound to Sam within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca504

b:33.0
occ:0.50
OD2 B:ASP279 2.4 37.4 1.0
O B:HOH719 2.4 31.3 0.5
O B:SER246 2.4 27.6 1.0
OG B:SER246 2.4 34.8 1.0
CB B:SER246 3.3 39.4 1.0
CG B:ASP279 3.3 31.8 1.0
C B:SER246 3.4 30.6 1.0
OD1 B:ASP279 3.6 31.3 1.0
CA B:SER246 3.8 34.6 1.0
O B:HOH648 4.4 47.5 1.0
O B:HOH782 4.6 46.1 1.0
N B:GLU247 4.6 37.9 1.0
CB B:ASP279 4.6 24.1 1.0
CB B:HIS281 4.9 27.2 1.0
ND1 B:HIS281 5.0 44.7 1.0

Calcium binding site 2 out of 2 in 5yf0

Go back to Calcium Binding Sites List in 5yf0
Calcium binding site 2 out of 2 in the Crystal Structure of CARNMT1 Bound to Sam


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of CARNMT1 Bound to Sam within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca505

b:0.8
occ:1.00
O B:HOH761 2.5 61.8 1.0
O B:HOH824 2.5 75.0 1.0
O B:HOH816 2.7 84.0 1.0
O B:HOH602 2.8 81.9 1.0
O B:HOH652 3.2 40.1 1.0
OD2 B:ASP110 3.4 42.7 1.0
OD1 B:ASP110 3.4 37.2 1.0
CG B:ASP110 3.8 40.6 1.0
OE2 B:GLU88 4.4 49.0 1.0
NH1 B:ARG113 4.6 23.9 1.0
OE1 B:GLU88 4.9 57.5 1.0
O B:LEU106 4.9 33.9 1.0

Reference:

R.Cao, X.Zhang, X.Liu, Y.Li, H.Li. Molecular Basis For Histidine N1 Position-Specific Methylation By CARNMT1. Cell Res. V. 28 494 2018.
ISSN: ISSN 1748-7838
PubMed: 29463897
DOI: 10.1038/S41422-018-0003-0
Page generated: Mon Jul 15 15:20:40 2024

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