Zinc in PDB 6vhf: Crystal Structure of RBBP5 Interacting Domain of CFP1

Protein crystallography data

The structure of Crystal Structure of RBBP5 Interacting Domain of CFP1, PDB code: 6vhf was solved by M.Joshi, J.F.Couture, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.03 / 2.31
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 67.266, 71.614, 78.132, 90.00, 90.00, 90.00
R / Rfree (%) 23.3 / 27.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of RBBP5 Interacting Domain of CFP1 (pdb code 6vhf). 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 Crystal Structure of RBBP5 Interacting Domain of CFP1, PDB code: 6vhf:

Zinc binding site 1 out of 1 in 6vhf

Go back to Zinc Binding Sites List in 6vhf
Zinc binding site 1 out of 1 in the Crystal Structure of RBBP5 Interacting Domain of CFP1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of RBBP5 Interacting Domain of CFP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:75.6
occ:1.00
ND1 A:HIS459 2.2 71.6 1.0
SG A:CYS456 2.4 70.5 1.0
SG A:CYS378 2.4 53.3 1.0
SG A:CYS451 2.6 62.7 1.0
CG A:HIS459 3.0 63.1 1.0
CE1 A:HIS459 3.1 67.5 1.0
CB A:CYS456 3.2 69.7 1.0
CB A:HIS459 3.2 61.7 1.0
CB A:CYS378 3.2 56.4 1.0
CB A:CYS451 3.6 61.1 1.0
CD2 A:HIS459 4.1 70.7 1.0
NE2 A:HIS459 4.1 68.1 1.0
N A:HIS459 4.2 72.8 1.0
CB A:TYR380 4.3 56.2 1.0
CA A:HIS459 4.3 69.1 1.0
CB A:ARG453 4.5 70.2 1.0
CA A:CYS456 4.7 75.2 1.0
CA A:CYS378 4.7 55.1 1.0
O A:CYS451 4.9 60.7 1.0
CA A:CYS451 4.9 56.8 1.0

Reference:

Y.Yang, M.Joshi, Y.H.Takahashi, Z.Ning, Q.Qu, J.S.Brunzelle, G.Skiniotis, D.Figeys, A.Shilatifard, J.F.Couture. A Non-Canonical Monovalent Zinc Finger Stabilizes the Integration of CFP1 Into the H3K4 Methyltransferase Complex Compass. Nucleic Acids Res. V. 48 421 2020.
ISSN: ESSN 1362-4962
PubMed: 31724694
DOI: 10.1093/NAR/GKZ1037
Page generated: Wed Dec 16 13:01:44 2020

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