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Magnesium in PDB 9di0: Cryo-Em Structure of KIF18A Bound to A Microtubule

Enzymatic activity of Cryo-Em Structure of KIF18A Bound to A Microtubule

All present enzymatic activity of Cryo-Em Structure of KIF18A Bound to A Microtubule:
2.1.1.63;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of KIF18A Bound to A Microtubule (pdb code 9di0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryo-Em Structure of KIF18A Bound to A Microtubule, PDB code: 9di0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 9di0

Go back to Magnesium Binding Sites List in 9di0
Magnesium binding site 1 out of 2 in the Cryo-Em Structure of KIF18A Bound to A Microtubule


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of KIF18A Bound to A Microtubule within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:47.4
occ:1.00
OG1 A:THR120 2.0 49.9 1.0
CB A:THR120 2.4 53.2 1.0
NH2 A:ARG227 2.4 41.5 1.0
CG2 A:THR120 2.6 46.8 1.0
CZ A:ARG227 2.6 39.8 1.0
O3A A:ADP601 2.9 68.5 1.0
NH1 A:ARG227 3.0 41.6 1.0
CG2 A:THR224 3.0 59.6 1.0
NE A:ARG227 3.3 34.4 1.0
O2B A:ADP601 3.5 59.1 1.0
CB A:THR224 3.6 62.0 1.0
O1A A:ADP601 3.7 68.1 1.0
PA A:ADP601 3.9 74.7 1.0
PB A:ADP601 3.9 72.9 1.0
CA A:THR120 3.9 52.7 1.0
OG1 A:THR224 4.2 60.3 1.0
CD A:ARG227 4.3 40.4 1.0
O3B A:ADP601 4.5 58.9 1.0
N A:THR120 4.5 49.8 1.0
O2A A:ADP601 4.5 63.9 1.0
C A:THR120 4.8 50.0 1.0
NZ A:LYS119 4.9 46.8 1.0
OD2 A:ASP258 4.9 34.4 1.0
CA A:THR224 4.9 61.8 1.0
OE1 A:GLN216 4.9 54.5 1.0
NH2 A:ARG214 4.9 25.5 1.0

Magnesium binding site 2 out of 2 in 9di0

Go back to Magnesium Binding Sites List in 9di0
Magnesium binding site 2 out of 2 in the Cryo-Em Structure of KIF18A Bound to A Microtubule


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryo-Em Structure of KIF18A Bound to A Microtubule within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Mg502

b:41.2
occ:1.00
OE2 L:GLU71 2.3 49.4 1.0
O1B L:GTP501 2.4 46.1 1.0
O1G L:GTP501 2.8 47.9 1.0
CD L:GLU71 3.4 47.4 1.0
PB L:GTP501 3.6 47.2 1.0
CG L:GLU71 3.8 42.0 1.0
O3B L:GTP501 3.8 44.0 1.0
PG L:GTP501 3.8 48.1 1.0
NZ K:LYS252 3.9 32.9 1.0
OD1 K:ASN247 4.0 46.5 1.0
OE1 L:GLN11 4.1 30.8 1.0
CB L:GLN11 4.2 20.3 1.0
O2B L:GTP501 4.4 36.6 1.0
O2G L:GTP501 4.4 41.6 1.0
OE1 L:GLU71 4.4 48.5 1.0
OD1 L:ASP69 4.6 41.7 1.0
OD2 L:ASP69 4.6 37.9 1.0
CB L:ASP98 4.6 45.9 1.0
CD L:GLN11 4.8 23.5 1.0
N L:GLN11 4.8 22.3 1.0
O3A L:GTP501 4.8 50.3 1.0
OD2 L:ASP98 4.9 49.2 1.0
O1A L:GTP501 4.9 34.5 1.0

Reference:

J.M.Perez-Bertoldi, Y.Zhao, A.Thawani, A.Yildiz, E.Nogales. Hurp Regulates KIF18A Recruitment and Activity to Synergistically Control Microtubule Dynamics. Nat Commun V. 15 9687 2024.
ISSN: ESSN 2041-1723
PubMed: 39516196
DOI: 10.1038/S41467-024-53691-7
Page generated: Sat Aug 16 00:37:09 2025

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