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Mercury in PDB 1ad2: Ribosomal Protein L1 Mutant with Serine 179 Replaced By Cysteine

Protein crystallography data

The structure of Ribosomal Protein L1 Mutant with Serine 179 Replaced By Cysteine, PDB code: 1ad2 was solved by J.Unge, S.Al-Karadaghi, A.Liljas, B.-H.Jonsson, I.Eliseikina, N.Ossina, N.Nevskaya, N.Fomenkova, M.Garber, S.Nikonov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 76.100, 61.400, 46.100, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 27

Mercury Binding Sites:

The binding sites of Mercury atom in the Ribosomal Protein L1 Mutant with Serine 179 Replaced By Cysteine (pdb code 1ad2). 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 Ribosomal Protein L1 Mutant with Serine 179 Replaced By Cysteine, PDB code: 1ad2:

Mercury binding site 1 out of 1 in 1ad2

Go back to Mercury Binding Sites List in 1ad2
Mercury binding site 1 out of 1 in the Ribosomal Protein L1 Mutant with Serine 179 Replaced By Cysteine


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Ribosomal Protein L1 Mutant with Serine 179 Replaced By Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg900

b:21.0
occ:0.20
NE2 A:HIS172 2.9 52.1 1.0
CD2 A:HIS172 3.4 46.2 1.0
OE2 A:GLU42 3.5 39.8 1.0
CE1 A:HIS172 4.0 51.1 1.0
OE1 A:GLU42 4.1 37.0 1.0
CD A:GLU42 4.2 33.2 1.0
CG A:HIS172 4.7 41.7 1.0
ND1 A:HIS172 5.0 47.0 1.0

Reference:

J.Unge, S.Al-Karadaghi, A.Liljas, B.H.Jonsson, I.Eliseikina, N.Ossina, N.Nevskaya, N.Fomenkova, M.Garber, S.Nikonov. A Mutant Form of the Ribosomal Protein L1 Reveals Conformational Flexibility. Febs Lett. V. 411 53 1997.
ISSN: ISSN 0014-5793
PubMed: 9247141
DOI: 10.1016/S0014-5793(97)00611-X
Page generated: Wed Oct 28 18:38:44 2020

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