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Samarium in PDB 5lxr: Structure of the Minimal RBM7 - ZCCHC8 Complex

Protein crystallography data

The structure of Structure of the Minimal RBM7 - ZCCHC8 Complex, PDB code: 5lxr was solved by S.Falk, K.Finogenova, C.Benda, E.Conti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 87.61 / 2.00
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 79.519, 79.519, 87.609, 90.00, 90.00, 120.00
R / Rfree (%) 20.2 / 22.9

Other elements in 5lxr:

The structure of Structure of the Minimal RBM7 - ZCCHC8 Complex also contains other interesting chemical elements:

Bromine (Br) 4 atoms
Chlorine (Cl) 1 atom

Samarium Binding Sites:

The binding sites of Samarium atom in the Structure of the Minimal RBM7 - ZCCHC8 Complex (pdb code 5lxr). This binding sites where shown within 5.0 Angstroms radius around Samarium atom.
In total 4 binding sites of Samarium where determined in the Structure of the Minimal RBM7 - ZCCHC8 Complex, PDB code: 5lxr:
Jump to Samarium binding site number: 1; 2; 3; 4;

Samarium binding site 1 out of 4 in 5lxr

Go back to Samarium Binding Sites List in 5lxr
Samarium binding site 1 out of 4 in the Structure of the Minimal RBM7 - ZCCHC8 Complex


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 1 of Structure of the Minimal RBM7 - ZCCHC8 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sm101

b:41.3
occ:1.00
OE1 A:GLU60 2.5 36.4 1.0
OE2 A:GLU60 2.5 38.5 1.0
OD2 A:ASP9 2.5 62.4 1.0
CD A:GLU60 2.8 39.9 1.0
CG A:ASP9 3.6 66.1 1.0
HB3 A:ASP9 4.0 77.9 1.0
SM A:SM102 4.1 58.3 0.3
OD1 A:ASP9 4.3 77.5 1.0
CG A:GLU60 4.4 41.3 1.0
CB A:ASP9 4.4 65.0 1.0
HG3 A:GLU60 4.7 49.6 1.0
HG2 A:GLU60 4.7 49.6 1.0
HB2 A:ASP9 4.9 77.9 1.0
HB2 A:GLU60 5.0 46.6 1.0

Samarium binding site 2 out of 4 in 5lxr

Go back to Samarium Binding Sites List in 5lxr
Samarium binding site 2 out of 4 in the Structure of the Minimal RBM7 - ZCCHC8 Complex


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 2 of Structure of the Minimal RBM7 - ZCCHC8 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sm102

b:58.3
occ:0.31
SM A:SM102 0.0 58.3 0.3
OD2 A:ASP9 2.6 62.4 1.0
SM A:SM102 2.9 0.9 0.7
HB2 A:ASP9 3.0 77.9 1.0
CG A:ASP9 3.2 66.1 1.0
CB A:ASP9 3.5 65.0 1.0
HB3 A:ASP9 3.6 77.9 1.0
OE2 A:GLU60 4.0 38.5 1.0
SM A:SM101 4.1 41.3 1.0
OD1 A:ASP9 4.1 77.5 1.0
H A:ASP9 4.7 71.7 1.0
CD A:GLU60 4.9 39.9 1.0
CA A:ASP9 5.0 57.5 1.0

Samarium binding site 3 out of 4 in 5lxr

Go back to Samarium Binding Sites List in 5lxr
Samarium binding site 3 out of 4 in the Structure of the Minimal RBM7 - ZCCHC8 Complex


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 3 of Structure of the Minimal RBM7 - ZCCHC8 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sm102

b:0.9
occ:0.69
SM A:SM102 0.0 0.9 0.7
SM A:SM102 2.9 58.3 0.3
HE A:ARG10 3.9 86.5 1.0
HB2 A:ASP9 4.3 77.9 1.0
HD3 A:ARG10 4.4 67.9 1.0
N A:GLU7 4.4 71.7 1.0
HG3 A:ARG10 4.5 65.2 1.0
NE A:ARG10 4.6 72.1 1.0
CD A:ARG10 4.9 56.6 1.0

Samarium binding site 4 out of 4 in 5lxr

Go back to Samarium Binding Sites List in 5lxr
Samarium binding site 4 out of 4 in the Structure of the Minimal RBM7 - ZCCHC8 Complex


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 4 of Structure of the Minimal RBM7 - ZCCHC8 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sm103

b:40.7
occ:1.00
O A:HOH218 1.9 41.5 1.0
OE2 A:GLU24 2.5 44.0 1.0
OE1 A:GLU24 2.6 38.2 1.0
O B:HOH504 2.6 41.5 1.0
CD A:GLU24 2.9 37.1 1.0
CG A:GLU24 4.4 39.6 1.0
O A:HOH240 4.7 55.1 1.0
HG3 A:GLU24 4.7 47.6 1.0
HG2 A:GLU24 4.8 47.6 1.0
OE2 B:GLU294 4.9 56.1 1.0
HB3 A:GLU24 5.0 49.3 1.0

Reference:

S.Falk, K.Finogenova, M.Melko, C.Benda, S.Lykke-Andersen, T.H.Jensen, E.Conti. Structure of the RBM7-ZCCHC8 Core of the Next Complex Reveals Connections to Splicing Factors. Nat Commun V. 7 13573 2016.
ISSN: ESSN 2041-1723
PubMed: 27905398
DOI: 10.1038/NCOMMS13573
Page generated: Thu Oct 10 13:57:02 2024

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