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Magnesium in PDB 6k7j: Cryo-Em Structure of the Human P4-Type Flippase ATP8A1-CDC50 (E1-Atp State CLASS1)

Enzymatic activity of Cryo-Em Structure of the Human P4-Type Flippase ATP8A1-CDC50 (E1-Atp State CLASS1)

All present enzymatic activity of Cryo-Em Structure of the Human P4-Type Flippase ATP8A1-CDC50 (E1-Atp State CLASS1):
7.6.2.1;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of the Human P4-Type Flippase ATP8A1-CDC50 (E1-Atp State CLASS1) (pdb code 6k7j). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Cryo-Em Structure of the Human P4-Type Flippase ATP8A1-CDC50 (E1-Atp State CLASS1), PDB code: 6k7j:

Magnesium binding site 1 out of 1 in 6k7j

Go back to Magnesium Binding Sites List in 6k7j
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of the Human P4-Type Flippase ATP8A1-CDC50 (E1-Atp State CLASS1)


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 the Human P4-Type Flippase ATP8A1-CDC50 (E1-Atp State CLASS1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1202

b:0.1
occ:1.00
OD2 A:ASP409 2.2 94.5 1.0
O A:THR411 2.4 0.8 1.0
O1G A:ACP1201 3.1 0.8 1.0
CG A:ASP409 3.4 94.5 1.0
C A:THR411 3.6 0.8 1.0
OD2 A:ASP790 3.6 90.1 1.0
O2G A:ACP1201 3.7 0.8 1.0
OG1 A:THR411 3.8 0.8 1.0
CB A:ASP786 3.9 93.1 1.0
PG A:ACP1201 4.0 0.8 1.0
OD1 A:ASP409 4.1 94.5 1.0
N A:GLY787 4.2 95.0 1.0
CB A:ASP409 4.4 94.5 1.0
N A:THR411 4.5 0.8 1.0
CA A:THR411 4.5 0.8 1.0
N A:GLY412 4.5 95.4 1.0
CG A:ASP790 4.6 90.1 1.0
CA A:GLY412 4.6 95.4 1.0
N A:ASP786 4.6 93.1 1.0
CA A:ASP786 4.7 93.1 1.0
OD1 A:ASP786 4.7 93.1 1.0
CB A:THR411 4.7 0.8 1.0
OD1 A:ASP790 4.8 90.1 1.0
CG A:ASP786 4.8 93.1 1.0
CA A:GLY787 4.8 95.0 1.0
C A:ASP786 4.8 93.1 1.0

Reference:

M.Hiraizumi, K.Yamashita, T.Nishizawa, O.Nureki. Cryo-Em Structures Capture the Transport Cycle of the P4-Atpase Flippase. Science V. 365 1149 2019.
ISSN: ESSN 1095-9203
PubMed: 31416931
DOI: 10.1126/SCIENCE.AAY3353
Page generated: Tue Oct 1 06:47:29 2024

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