Bromine in PDB 8p75: Cryo-Em Structure of Cak in Complex with Inhibitor ICEC0880 (Ring-Down Conformation)

Enzymatic activity of Cryo-Em Structure of Cak in Complex with Inhibitor ICEC0880 (Ring-Down Conformation)

All present enzymatic activity of Cryo-Em Structure of Cak in Complex with Inhibitor ICEC0880 (Ring-Down Conformation):
2.7.11.22; 2.7.11.23;

Bromine Binding Sites:

The binding sites of Bromine atom in the Cryo-Em Structure of Cak in Complex with Inhibitor ICEC0880 (Ring-Down Conformation) (pdb code 8p75). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Cryo-Em Structure of Cak in Complex with Inhibitor ICEC0880 (Ring-Down Conformation), PDB code: 8p75:

Bromine binding site 1 out of 1 in 8p75

Go back to Bromine Binding Sites List in 8p75
Bromine binding site 1 out of 1 in the Cryo-Em Structure of Cak in Complex with Inhibitor ICEC0880 (Ring-Down Conformation)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Cryo-Em Structure of Cak in Complex with Inhibitor ICEC0880 (Ring-Down Conformation) within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Br401

b:75.5
occ:1.00
BR17 J:X3Z401 0.0 75.5 1.0
C16 J:X3Z401 1.9 37.9 1.0
C11 J:X3Z401 2.9 33.9 1.0
C15 J:X3Z401 2.9 34.3 1.0
C10 J:X3Z401 3.1 34.2 1.0
O J:HOH516 3.2 41.6 1.0
C18 J:X3Z401 3.9 34.1 1.0
OD1 J:ASP97 4.1 31.1 1.0
C12 J:X3Z401 4.2 35.3 1.0
C14 J:X3Z401 4.2 37.1 1.0
N09 J:X3Z401 4.3 37.3 1.0
O J:HOH510 4.4 23.6 1.0
CG J:ASP97 4.4 28.1 1.0
C08 J:X3Z401 4.6 36.3 1.0
C13 J:X3Z401 4.7 36.1 1.0
OD2 J:ASP97 4.8 28.4 1.0
CG2 J:VAL100 4.8 21.7 1.0
C19 J:X3Z401 4.9 34.5 1.0
CB J:ASP97 5.0 16.3 1.0
N20 J:X3Z401 5.0 34.8 1.0

Reference:

V.I.Cushing, A.F.Koh, J.Feng, K.Jurgaityte, A.Bondke, S.H.B.Kroll, M.Barbazanges, B.Scheiper, A.K.Bahl, A.G.M.Barrett, S.Ali, A.Kotecha, B.J.Greber. High-Resolution Cryo-Em of the Human Cdk-Activating Kinase For Structure-Based Drug Design Nat Commun 2024.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-024-46375-9
Page generated: Thu Jul 11 05:28:03 2024

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