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Aluminium in PDB 9mx5: Cryo-Em Structure of Ancestral Dicer Helicase Bound to 27-Bp Dsrna in Internally-Bound Transition State

Other elements in 9mx5:

The structure of Cryo-Em Structure of Ancestral Dicer Helicase Bound to 27-Bp Dsrna in Internally-Bound Transition State also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Magnesium (Mg) 1 atom

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Cryo-Em Structure of Ancestral Dicer Helicase Bound to 27-Bp Dsrna in Internally-Bound Transition State (pdb code 9mx5). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Cryo-Em Structure of Ancestral Dicer Helicase Bound to 27-Bp Dsrna in Internally-Bound Transition State, PDB code: 9mx5:

Aluminium binding site 1 out of 1 in 9mx5

Go back to Aluminium Binding Sites List in 9mx5
Aluminium binding site 1 out of 1 in the Cryo-Em Structure of Ancestral Dicer Helicase Bound to 27-Bp Dsrna in Internally-Bound Transition State


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Cryo-Em Structure of Ancestral Dicer Helicase Bound to 27-Bp Dsrna in Internally-Bound Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al701

b:112.7
occ:1.00
AL A:AF3701 0.0 112.7 1.0
F1 A:AF3701 1.6 102.1 1.0
F2 A:AF3701 1.6 99.5 1.0
F3 A:AF3701 1.6 115.8 1.0
O3B A:ADP702 2.5 96.6 1.0
O1B A:ADP702 2.8 96.3 1.0
PB A:ADP702 3.1 95.3 1.0
O3A A:ADP702 3.6 108.3 1.0
MG A:MG703 4.1 83.0 1.0
NH2 A:ARG480 4.1 101.7 1.0
N A:GLY34 4.5 94.8 1.0
O2B A:ADP702 4.5 94.9 1.0
NH2 A:ARG478 4.5 92.8 1.0
NZ A:LYS37 4.6 91.5 1.0
CA A:THR33 4.7 90.1 1.0
CE A:LYS37 4.7 90.7 1.0
CB A:THR33 4.8 83.9 1.0
CA A:GLY451 4.9 96.4 1.0
OE2 A:GLU143 5.0 111.1 1.0

Reference:

A.M.Aderounmu, J.Maus-Conn, C.D.Consalvo, P.S.Shen, B.L.Bass. Biochemical and Structural Basis of Dicer Helicase Function Unveiled By Resurrecting Ancient Proteins. Biorxiv 2025.
ISSN: ISSN 2692-8205
PubMed: 39990435
DOI: 10.1101/2025.02.15.638221
Page generated: Sun Jul 6 22:42:00 2025

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