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Mercury in PDB 1l8d: RAD50 Coiled-Coil Zn Hook

Protein crystallography data

The structure of RAD50 Coiled-Coil Zn Hook, PDB code: 1l8d was solved by K.P.Hopfner, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 31.958, 77.868, 53.330, 90.00, 91.55, 90.00
R / Rfree (%) 22.5 / 27.8

Mercury Binding Sites:

The binding sites of Mercury atom in the RAD50 Coiled-Coil Zn Hook (pdb code 1l8d). 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 RAD50 Coiled-Coil Zn Hook, PDB code: 1l8d:

Mercury binding site 1 out of 1 in 1l8d

Go back to Mercury Binding Sites List in 1l8d
Mercury binding site 1 out of 1 in the RAD50 Coiled-Coil Zn Hook


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of RAD50 Coiled-Coil Zn Hook within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg201

b:35.3
occ:1.00
SG B:CYS444 2.3 31.3 1.0
SG A:CYS444 2.4 29.8 1.0
SG A:CYS447 2.5 42.1 1.0
SG B:CYS447 2.5 39.2 1.0
CB A:CYS447 3.2 39.3 1.0
CB B:CYS444 3.3 34.3 1.0
CB A:CYS444 3.3 32.4 1.0
CB B:CYS447 3.5 37.2 1.0
N A:CYS447 3.7 38.1 1.0
N B:CYS447 3.7 35.8 1.0
CA A:CYS447 4.0 38.5 1.0
CA B:CYS447 4.2 36.9 1.0
CB B:VAL446 4.4 34.3 1.0
CB A:VAL446 4.6 37.6 1.0
CA B:CYS444 4.7 36.6 1.0
C B:VAL446 4.7 36.7 1.0
CA A:CYS444 4.7 33.7 1.0
CG1 B:VAL446 4.8 35.2 1.0
NH2 A:ARG449 4.8 52.0 1.0
C A:VAL446 4.8 38.9 1.0
C A:CYS447 4.8 37.6 1.0
CG1 A:VAL446 4.9 37.0 1.0
CA B:VAL446 4.9 35.7 1.0
C B:CYS447 4.9 38.9 1.0
N B:VAL446 5.0 36.2 1.0

Reference:

K.P.Hopfner, L.Craig, G.Moncalian, R.A.Zinkel, T.Usui, B.A.Owen, A.Karcher, B.Henderson, J.L.Bodmer, C.T.Mcmurray, J.P.Carney, J.H.Petrini, J.A.Tainer. The RAD50 Zinc-Hook Is A Structure Joining MRE11 Complexes in Dna Recombination and Repair. Nature V. 418 562 2002.
ISSN: ISSN 0028-0836
PubMed: 12152085
DOI: 10.1038/NATURE00922
Page generated: Sun Dec 13 19:03:45 2020

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