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Mercury in PDB 357d: 3.5 A Structure of Fragment I From E. Coli 5S Rrna

Protein crystallography data

The structure of 3.5 A Structure of Fragment I From E. Coli 5S Rrna, PDB code: 357d was solved by C.C.Correll, B.Freeborn, P.B.Moore, T.A.Steitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 3.50
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 58.670, 58.670, 248.840, 90.00, 90.00, 120.00
R / Rfree (%) 31.2 / 26.5

Other elements in 357d:

The structure of 3.5 A Structure of Fragment I From E. Coli 5S Rrna also contains other interesting chemical elements:

Magnesium (Mg) 8 atoms

Mercury Binding Sites:

The binding sites of Mercury atom in the 3.5 A Structure of Fragment I From E. Coli 5S Rrna (pdb code 357d). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the 3.5 A Structure of Fragment I From E. Coli 5S Rrna, PDB code: 357d:

Mercury binding site 1 out of 1 in 357d

Go back to Mercury Binding Sites List in 357d
Mercury binding site 1 out of 1 in the 3.5 A Structure of Fragment I From E. Coli 5S Rrna


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of 3.5 A Structure of Fragment I From E. Coli 5S Rrna within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg89

b:0.8
occ:1.00
N3 B:U74 2.7 53.0 1.0
C2 B:U74 3.4 51.7 1.0
C4 B:U74 3.5 51.5 1.0
O2 B:U74 3.5 53.0 1.0
O4 B:U74 3.6 49.2 1.0
N6 B:A73 3.7 48.7 1.0
N1 B:A73 3.9 47.7 1.0
C6 B:A73 4.0 47.5 1.0
N3 B:G75 4.2 54.9 1.0
C4 B:G75 4.3 53.5 1.0
N1 B:U74 4.5 49.9 1.0
C2 B:G75 4.6 55.5 1.0
C5 B:U74 4.6 50.5 1.0
O2 C:U103 4.6 72.5 1.0
N9 B:G75 4.6 53.9 1.0
C5 B:G75 4.8 52.8 1.0
C2 B:A73 4.8 44.5 1.0
C1' B:G75 4.9 55.5 1.0
C5 B:A73 5.0 45.8 1.0
C6 B:U74 5.0 50.0 1.0
N1 B:G75 5.0 53.6 1.0

Reference:

C.C.Correll, B.Freeborn, P.B.Moore, T.A.Steitz. Metals, Motifs, and Recognition in the Crystal Structure of A 5S Rrna Domain. Cell(Cambridge,Mass.) V. 91 705 1997.
ISSN: ISSN 0092-8674
PubMed: 9393863
DOI: 10.1016/S0092-8674(00)80457-2
Page generated: Wed Oct 28 18:42:09 2020

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