Magnesium in PDB 6c90: Human MTR4 Helicase in Complex with ZCCHC8-Ctd

Enzymatic activity of Human MTR4 Helicase in Complex with ZCCHC8-Ctd

All present enzymatic activity of Human MTR4 Helicase in Complex with ZCCHC8-Ctd:
3.6.4.13;

Protein crystallography data

The structure of Human MTR4 Helicase in Complex with ZCCHC8-Ctd, PDB code: 6c90 was solved by M.R.Puno, C.D.Lima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 73.80 / 2.20
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 147.635, 147.635, 101.589, 90.00, 90.00, 120.00
R / Rfree (%) 19 / 22.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human MTR4 Helicase in Complex with ZCCHC8-Ctd (pdb code 6c90). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human MTR4 Helicase in Complex with ZCCHC8-Ctd, PDB code: 6c90:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6c90

Go back to Magnesium Binding Sites List in 6c90
Magnesium binding site 1 out of 2 in the Human MTR4 Helicase in Complex with ZCCHC8-Ctd


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human MTR4 Helicase in Complex with ZCCHC8-Ctd within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1102

b:68.8
occ:1.00
O A:HOH1347 3.0 51.9 1.0
O4 A:TLA1108 3.1 66.9 1.0
CB A:SER555 4.0 84.4 1.0
OG A:SER555 4.2 82.2 1.0
C4 A:TLA1108 4.2 66.6 1.0
CB A:PRO287 4.2 33.4 1.0
CA A:PRO287 4.4 32.2 1.0
O41 A:TLA1108 4.5 67.6 1.0
OH A:TYR308 4.6 46.3 1.0
O A:HOH1395 5.0 53.4 1.0

Magnesium binding site 2 out of 2 in 6c90

Go back to Magnesium Binding Sites List in 6c90
Magnesium binding site 2 out of 2 in the Human MTR4 Helicase in Complex with ZCCHC8-Ctd


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human MTR4 Helicase in Complex with ZCCHC8-Ctd within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1103

b:36.3
occ:1.00
O A:VAL576 2.2 37.9 1.0
O A:ILE579 2.2 41.1 1.0
O A:HOH1379 2.3 35.7 1.0
O A:LEU573 2.3 32.3 1.0
O A:HOH1399 2.4 44.9 1.0
O A:LEU574 2.6 31.8 1.0
C A:LEU574 3.2 29.5 1.0
C A:VAL576 3.3 37.7 1.0
C A:ILE579 3.4 39.7 1.0
C A:LEU573 3.5 33.8 1.0
CA A:LEU574 3.5 38.1 1.0
N A:LEU574 3.9 34.4 1.0
N A:VAL576 4.0 38.3 1.0
O A:HOH1252 4.1 44.5 1.0
C A:ARG575 4.2 37.0 1.0
N A:ARG575 4.2 35.4 1.0
N A:ILE579 4.2 48.9 1.0
N A:GLU577 4.2 45.6 1.0
CA A:VAL576 4.2 38.9 1.0
CA A:GLU577 4.2 55.6 1.0
CG2 A:ILE579 4.3 38.5 1.0
CA A:ASN580 4.3 40.9 1.0
N A:ASN580 4.3 37.8 1.0
CA A:ILE579 4.4 40.2 1.0
O A:ARG575 4.5 43.5 1.0
O A:HOH1319 4.6 48.3 1.0
C A:GLU577 4.7 47.4 1.0
CA A:LEU573 4.7 38.1 1.0
O A:HOH1409 4.8 57.9 1.0
CA A:ARG575 4.8 38.6 1.0
N A:GLU578 4.8 44.9 1.0
CB A:ASN580 4.8 44.3 1.0
CB A:LEU574 4.9 28.2 1.0
CB A:VAL576 4.9 35.0 1.0

Reference:

M.R.Puno, C.D.Lima. Structural Basis For MTR4-ZCCHC8 Interactions That Stimulate the MTR4 Helicase in the Nuclear Exosome-Targeting Complex. Proc. Natl. Acad. Sci. V. 115 E5506 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29844170
DOI: 10.1073/PNAS.1803530115
Page generated: Mon Dec 14 22:26:54 2020

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