Zinc in PDB 5tab: Crystal Structure of the Phd Finger of PHF20

Protein crystallography data

The structure of Crystal Structure of the Phd Finger of PHF20, PDB code: 5tab was solved by B.J.Klein, T.G.Kutateladze, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.69 / 1.25
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 46.739, 46.739, 50.928, 90.00, 90.00, 120.00
R / Rfree (%) 11.8 / 14.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Phd Finger of PHF20 (pdb code 5tab). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Phd Finger of PHF20, PDB code: 5tab:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5tab

Go back to Zinc Binding Sites List in 5tab
Zinc binding site 1 out of 2 in the Crystal Structure of the Phd Finger of PHF20


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 the Phd Finger of PHF20 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn101

b:7.7
occ:0.86
SG A:CYS52 2.3 9.1 0.8
SG A:CYS49 2.3 8.1 0.9
SG A:CYS24 2.4 8.2 0.9
SG A:CYS27 2.4 8.7 0.9
CB A:CYS24 3.2 8.2 1.0
CB A:CYS52 3.2 9.3 0.9
CB A:CYS27 3.3 10.9 1.0
CB A:CYS49 3.5 7.8 1.0
N A:CYS27 3.7 11.3 1.0
N A:CYS49 3.9 7.3 0.9
NH2 A:ARG9 4.1 10.7 0.9
CA A:CYS27 4.1 10.7 1.0
N A:CYS52 4.2 9.6 1.0
CA A:CYS49 4.2 8.3 1.0
CA A:CYS52 4.3 9.0 0.8
NH1 A:ARG9 4.5 9.3 1.0
CB A:GLU26 4.6 17.8 1.0
CA A:CYS24 4.6 7.1 1.0
C A:CYS49 4.8 7.7 1.0
C A:GLU26 4.8 13.5 1.0
CZ A:ARG9 4.8 8.7 0.8
C A:CYS27 4.9 9.6 1.0
O A:CYS49 4.9 9.1 1.0
CB A:VAL51 4.9 9.6 1.0
OG A:SER29 5.0 8.7 0.9
N A:GLN28 5.0 8.6 0.9

Zinc binding site 2 out of 2 in 5tab

Go back to Zinc Binding Sites List in 5tab
Zinc binding site 2 out of 2 in the Crystal Structure of the Phd Finger of PHF20


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Phd Finger of PHF20 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn102

b:6.9
occ:0.90
ND1 A:HIS32 2.1 8.3 1.0
SG A:CYS12 2.3 8.7 1.0
SG A:CYS35 2.3 7.5 0.9
SG A:CYS10 2.3 7.5 1.0
CE1 A:HIS32 3.0 9.1 0.9
CG A:HIS32 3.1 7.1 1.0
CB A:CYS10 3.2 7.7 1.0
CB A:CYS35 3.2 7.0 1.0
CB A:CYS12 3.3 10.3 1.0
CB A:HIS32 3.5 7.0 0.9
N A:CYS12 4.0 7.4 0.9
N A:HIS32 4.1 6.2 0.9
NE2 A:HIS32 4.2 8.9 0.9
CD2 A:HIS32 4.2 9.4 0.9
CA A:CYS12 4.3 9.3 1.0
CA A:HIS32 4.4 6.0 1.0
CA A:CYS10 4.5 7.6 1.0
CA A:CYS35 4.6 7.0 1.0
N A:ILE11 4.6 8.3 1.0
C A:CYS10 4.7 8.4 1.0
O A:HIS32 4.7 6.5 1.0
N A:CYS35 5.0 6.5 0.9

Reference:

B.J.Klein, X.Wang, G.Cui, C.Yuan, M.V.Botuyan, K.Lin, Y.Lu, X.Wang, Y.Zhao, C.J.Bruns, G.Mer, X.Shi, T.G.Kutateladze. PHF20 Readers Link Methylation of Histone H3K4 and P53 with H4K16 Acetylation. Cell Rep V. 17 1158 2016.
ISSN: ESSN 2211-1247
PubMed: 27760318
DOI: 10.1016/J.CELREP.2016.09.056
Page generated: Wed Dec 16 10:55:21 2020

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