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Magnesium in PDB 6lzj: Aquifex Aeolicus Mutl Atpase Domain Complexed with Amppcp

Protein crystallography data

The structure of Aquifex Aeolicus Mutl Atpase Domain Complexed with Amppcp, PDB code: 6lzj was solved by K.Fukui, K.Izuhara, T.Yano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.85 / 1.73
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 35.016, 42.863, 53.859, 81.11, 71.60, 77.69
R / Rfree (%) 20.9 / 23.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Aquifex Aeolicus Mutl Atpase Domain Complexed with Amppcp (pdb code 6lzj). 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 Aquifex Aeolicus Mutl Atpase Domain Complexed with Amppcp, PDB code: 6lzj:

Magnesium binding site 1 out of 1 in 6lzj

Go back to Magnesium Binding Sites List in 6lzj
Magnesium binding site 1 out of 1 in the Aquifex Aeolicus Mutl Atpase Domain Complexed with Amppcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Aquifex Aeolicus Mutl Atpase Domain Complexed with Amppcp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:32.5
occ:1.00
O1G A:ACP402 2.0 47.4 1.0
ND2 A:ASN26 2.0 21.0 1.0
O1B A:ACP402 2.1 24.5 1.0
O1A A:ACP402 2.1 26.8 1.0
O A:HOH513 2.1 23.1 1.0
O A:HOH526 2.2 24.6 1.0
PB A:ACP402 3.0 28.7 1.0
CG A:ASN26 3.0 17.0 1.0
PG A:ACP402 3.3 49.2 1.0
PA A:ACP402 3.3 26.6 1.0
OD1 A:ASN26 3.3 21.8 1.0
O3A A:ACP402 3.5 27.6 1.0
C3B A:ACP402 3.8 34.5 1.0
O A:HOH558 3.9 27.0 1.0
O5' A:ACP402 4.0 28.6 1.0
O3G A:ACP402 4.0 52.6 1.0
OE1 A:GLU25 4.1 27.4 1.0
OE1 A:GLU22 4.2 24.9 1.0
CB A:ALA91 4.3 41.7 1.0
CB A:ASN26 4.4 19.8 1.0
O2B A:ACP402 4.5 32.0 1.0
O A:GLU22 4.5 15.7 1.0
OD2 A:ASP29 4.5 27.0 1.0
O2G A:ACP402 4.5 48.1 1.0
O2A A:ACP402 4.5 24.8 1.0
CA A:ASN26 4.6 20.0 1.0
O A:HOH565 4.7 43.9 1.0
N A:ASN26 4.7 16.6 1.0
CD A:GLU25 4.9 29.3 1.0

Reference:

K.Izuhara, K.Fukui, T.Murakawa, S.Baba, T.Kumasaka, K.Uchiyama, T.Yano. A Lynch Syndrome-Associated Mutation at A Bergerat Atp-Binding Fold Destabilizes the Structure of the Dna Mismatch Repair Endonuclease Mutl. J.Biol.Chem. V. 295 11643 2020.
ISSN: ESSN 1083-351X
PubMed: 32571878
DOI: 10.1074/JBC.RA120.013576
Page generated: Tue Oct 1 10:49:59 2024

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