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Zinc in PDB 5gox: Eukaryotic RAD50 Functions As A Rod-Shaped Dimer

Protein crystallography data

The structure of Eukaryotic RAD50 Functions As A Rod-Shaped Dimer, PDB code: 5gox was solved by Y.B.Park, M.Hohl, M.Padjasek, E.Jeong, K.S.Jin, A.Krezel, J.H.J.Petrini, Y.Cho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.22 / 2.41
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.180, 61.972, 81.540, 90.00, 99.75, 90.00
R / Rfree (%) 21.3 / 27.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Eukaryotic RAD50 Functions As A Rod-Shaped Dimer (pdb code 5gox). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Eukaryotic RAD50 Functions As A Rod-Shaped Dimer, PDB code: 5gox:

Zinc binding site 1 out of 1 in 5gox

Go back to Zinc Binding Sites List in 5gox
Zinc binding site 1 out of 1 in the Eukaryotic RAD50 Functions As A Rod-Shaped Dimer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Eukaryotic RAD50 Functions As A Rod-Shaped Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn803

b:0.8
occ:1.00
SG A:CYS681 2.2 0.7 1.0
SG A:CYS684 2.2 0.3 1.0
SG B:CYS681 2.2 0.7 1.0
SG B:CYS684 2.2 0.3 1.0
CB A:CYS681 3.2 96.8 1.0
CB B:CYS684 3.3 95.1 1.0
CB B:CYS681 3.4 0.8 1.0
CB A:CYS684 3.5 0.1 1.0
N B:CYS684 3.6 0.3 1.0
N A:CYS684 3.9 0.1 1.0
CA B:CYS684 4.1 98.4 1.0
CA A:CYS684 4.3 0.1 1.0
CB B:VAL683 4.5 91.7 1.0
NH2 A:ARG686 4.6 0.9 1.0
CB A:VAL683 4.6 84.1 1.0
CA A:CYS681 4.7 96.5 1.0
C B:VAL683 4.7 0.0 1.0
CA B:CYS681 4.8 0.9 1.0
NE A:ARG686 4.8 0.6 1.0
N B:VAL683 4.9 96.3 1.0
C B:CYS684 4.9 0.1 1.0
CA B:VAL683 4.9 96.0 1.0
C A:VAL683 4.9 93.6 1.0
C A:CYS684 4.9 0.5 1.0
CG1 B:VAL683 5.0 93.3 1.0
N A:VAL683 5.0 87.2 1.0

Reference:

Y.B.Park, M.Hohl, M.Padjasek, E.Jeong, K.S.Jin, A.Krezel, J.H.J.Petrini, Y.Cho. Eukaryotic RAD50 Functions As A Rod-Shaped Dimer Nat. Struct. Mol. Biol. V. 24 248 2017.
ISSN: ESSN 1545-9985
PubMed: 28134932
DOI: 10.1038/NSMB.3369
Page generated: Wed Dec 16 06:19:40 2020

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