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Calcium in PDB 8ihn: Cryo-Em Structure of the RPD3S Core Complex

Enzymatic activity of Cryo-Em Structure of the RPD3S Core Complex

All present enzymatic activity of Cryo-Em Structure of the RPD3S Core Complex:
3.5.1.98;

Other elements in 8ihn:

The structure of Cryo-Em Structure of the RPD3S Core Complex also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Cryo-Em Structure of the RPD3S Core Complex (pdb code 8ihn). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Cryo-Em Structure of the RPD3S Core Complex, PDB code: 8ihn:

Calcium binding site 1 out of 1 in 8ihn

Go back to Calcium Binding Sites List in 8ihn
Calcium binding site 1 out of 1 in the Cryo-Em Structure of the RPD3S Core Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cryo-Em Structure of the RPD3S Core Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Ca502

b:70.0
occ:1.00
O L:VAL203 2.6 55.9 1.0
O L:PHE197 2.7 57.5 1.0
O L:TYR232 2.7 65.3 1.0
O L:THR200 3.2 64.0 1.0
C L:TYR232 3.7 65.3 1.0
C L:PHE197 3.7 57.5 1.0
C L:VAL203 3.8 55.9 1.0
CB L:TYR232 3.9 65.3 1.0
O L:TYR198 4.0 64.5 1.0
CA L:TYR198 4.2 64.5 1.0
C L:TYR198 4.3 64.5 1.0
N L:TYR198 4.4 64.5 1.0
C L:THR200 4.4 64.0 1.0
CA L:MET204 4.4 59.6 1.0
CB L:PHE197 4.4 57.5 1.0
CA L:TYR232 4.5 65.3 1.0
N L:ALA233 4.5 62.3 1.0
N L:MET204 4.6 59.6 1.0
CA L:ALA233 4.7 62.3 1.0
N L:THR205 4.7 57.0 1.0
CB L:ALA233 4.7 62.3 1.0
CA L:PHE197 4.7 57.5 1.0
OG1 L:THR205 4.7 57.0 1.0
O L:GLY229 4.8 67.5 1.0
CA L:VAL203 4.8 55.9 1.0
CA L:GLY229 4.9 67.5 1.0
CG2 L:THR200 4.9 64.0 1.0
CG2 L:THR205 4.9 57.0 1.0
CB L:VAL203 5.0 55.9 1.0
N L:VAL203 5.0 55.9 1.0

Reference:

Y.Zhang, M.Xu, P.Wang, J.Zhou, G.Wang, S.Han, G.Cai, X.Wang. Structural Basis For Nucleosome Binding and Catalysis By the Yeast RPD3S/Hdac Holoenzyme. Cell Res. V. 33 971 2023.
ISSN: ISSN 1001-0602
PubMed: 37845487
DOI: 10.1038/S41422-023-00884-2
Page generated: Thu Jul 10 05:13:29 2025

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