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Yttrium in PDB 3sah: Crystal Structure of the Human RRP6 Catalytic Domain with Y436A Mutation in the Catalytic Site

Protein crystallography data

The structure of Crystal Structure of the Human RRP6 Catalytic Domain with Y436A Mutation in the Catalytic Site, PDB code: 3sah was solved by K.Januszyk, Q.Liu, C.D.Lima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.99 / 2.65
Space group P 4
Cell size a, b, c (Å), α, β, γ (°) 141.000, 141.000, 58.400, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 26.5

Other elements in 3sah:

The structure of Crystal Structure of the Human RRP6 Catalytic Domain with Y436A Mutation in the Catalytic Site also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Yttrium Binding Sites:

The binding sites of Yttrium atom in the Crystal Structure of the Human RRP6 Catalytic Domain with Y436A Mutation in the Catalytic Site (pdb code 3sah). This binding sites where shown within 5.0 Angstroms radius around Yttrium atom.
In total 3 binding sites of Yttrium where determined in the Crystal Structure of the Human RRP6 Catalytic Domain with Y436A Mutation in the Catalytic Site, PDB code: 3sah:
Jump to Yttrium binding site number: 1; 2; 3;

Yttrium binding site 1 out of 3 in 3sah

Go back to Yttrium Binding Sites List in 3sah
Yttrium binding site 1 out of 3 in the Crystal Structure of the Human RRP6 Catalytic Domain with Y436A Mutation in the Catalytic Site


Mono view


Stereo pair view

A full contact list of Yttrium with other atoms in the Y binding site number 1 of Crystal Structure of the Human RRP6 Catalytic Domain with Y436A Mutation in the Catalytic Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Y1

b:0.4
occ:1.00
OE2 A:GLU489 1.9 82.7 1.0
OD1 A:ASP488 2.6 90.5 1.0
CD A:GLU489 3.0 83.2 1.0
OD2 A:ASP488 3.1 88.2 1.0
CG A:ASP488 3.2 88.6 1.0
OE1 A:GLU489 3.5 81.8 1.0
OE1 A:GLN511 3.9 71.8 1.0
CD A:GLN511 4.3 71.8 1.0
CG A:GLU489 4.3 82.4 1.0
O A:HOH607 4.6 46.8 1.0
CG A:GLN511 4.6 67.7 1.0
CB A:ASP488 4.7 87.2 1.0
N A:GLU489 4.8 84.3 1.0
NE2 A:GLN511 5.0 74.3 1.0
N A:ASP488 5.0 84.2 1.0

Yttrium binding site 2 out of 3 in 3sah

Go back to Yttrium Binding Sites List in 3sah
Yttrium binding site 2 out of 3 in the Crystal Structure of the Human RRP6 Catalytic Domain with Y436A Mutation in the Catalytic Site


Mono view


Stereo pair view

A full contact list of Yttrium with other atoms in the Y binding site number 2 of Crystal Structure of the Human RRP6 Catalytic Domain with Y436A Mutation in the Catalytic Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Y3

b:75.9
occ:1.00
OE2 A:GLU315 2.3 61.7 1.0
OD2 A:ASP440 2.5 65.6 1.0
CD A:GLU315 3.0 58.9 1.0
OE1 A:GLU315 3.0 57.4 1.0
CG A:ASP440 3.7 64.6 1.0
O A:HOH58 3.9 49.5 1.0
OD1 A:ASP440 4.2 66.4 1.0
OD2 A:ASP313 4.2 59.1 1.0
O A:LEU314 4.4 55.9 1.0
CG A:GLU315 4.5 56.9 1.0
CZ2 A:TRP424 4.5 45.4 1.0
O A:GLN418 4.6 83.9 1.0
OE1 A:GLN330 4.8 59.5 1.0
O A:ALA436 4.8 58.7 1.0
CB A:ASP440 4.9 63.5 1.0

Yttrium binding site 3 out of 3 in 3sah

Go back to Yttrium Binding Sites List in 3sah
Yttrium binding site 3 out of 3 in the Crystal Structure of the Human RRP6 Catalytic Domain with Y436A Mutation in the Catalytic Site


Mono view


Stereo pair view

A full contact list of Yttrium with other atoms in the Y binding site number 3 of Crystal Structure of the Human RRP6 Catalytic Domain with Y436A Mutation in the Catalytic Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Y607

b:59.2
occ:1.00
OE2 B:GLU489 2.1 74.3 1.0
OE1 B:GLU489 2.3 73.6 1.0
OD1 B:ASP488 2.4 67.8 1.0
O B:HOH52 2.5 38.5 1.0
CD B:GLU489 2.5 74.0 1.0
O B:HOH7 2.7 37.0 1.0
CG B:ASP488 3.3 65.7 1.0
OD2 B:ASP488 3.5 63.8 1.0
CG B:GLU489 4.0 75.1 1.0
O B:HOH84 4.5 41.0 1.0
N B:GLU489 4.6 72.4 1.0
CB B:ASP488 4.7 67.6 1.0
OE1 B:GLN511 4.8 58.7 1.0
CG B:GLN511 4.9 57.1 1.0
CB B:GLU489 5.0 74.8 1.0

Reference:

K.Januszyk, Q.Liu, C.D.Lima. Activities of Human RRP6 and Structure of the Human RRP6 Catalytic Domain. Rna V. 17 1566 2011.
ISSN: ISSN 1355-8382
PubMed: 21705430
DOI: 10.1261/RNA.2763111
Page generated: Mon Jan 25 16:07:20 2021

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