Magnesium in PDB 6wgv: Mycobacterium Tuberculosis Pduo-Type Atp:Cobalamin Adenosyltransferase Bound to Adenosylcobalamin and Pppi

Enzymatic activity of Mycobacterium Tuberculosis Pduo-Type Atp:Cobalamin Adenosyltransferase Bound to Adenosylcobalamin and Pppi

All present enzymatic activity of Mycobacterium Tuberculosis Pduo-Type Atp:Cobalamin Adenosyltransferase Bound to Adenosylcobalamin and Pppi:
2.5.1.17;

Protein crystallography data

The structure of Mycobacterium Tuberculosis Pduo-Type Atp:Cobalamin Adenosyltransferase Bound to Adenosylcobalamin and Pppi, PDB code: 6wgv was solved by R.N.Mascarenhas, M.Ruetz, M.Koutmos, R.Banerjee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.68 / 2.15
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 87.631, 87.631, 46.554, 90, 90, 120
R / Rfree (%) 18.8 / 22.1

Other elements in 6wgv:

The structure of Mycobacterium Tuberculosis Pduo-Type Atp:Cobalamin Adenosyltransferase Bound to Adenosylcobalamin and Pppi also contains other interesting chemical elements:

Cobalt (Co) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mycobacterium Tuberculosis Pduo-Type Atp:Cobalamin Adenosyltransferase Bound to Adenosylcobalamin and Pppi (pdb code 6wgv). 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 Mycobacterium Tuberculosis Pduo-Type Atp:Cobalamin Adenosyltransferase Bound to Adenosylcobalamin and Pppi, PDB code: 6wgv:

Magnesium binding site 1 out of 1 in 6wgv

Go back to Magnesium Binding Sites List in 6wgv
Magnesium binding site 1 out of 1 in the Mycobacterium Tuberculosis Pduo-Type Atp:Cobalamin Adenosyltransferase Bound to Adenosylcobalamin and Pppi


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mycobacterium Tuberculosis Pduo-Type Atp:Cobalamin Adenosyltransferase Bound to Adenosylcobalamin and Pppi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg204

b:54.2
occ:1.00
O3G A:3PO203 1.7 87.4 1.0
OD1 A:ASN163 2.0 40.7 1.0
O A:HOH307 2.1 41.9 1.0
O A:HOH303 2.3 39.9 1.0
O1B A:3PO203 2.4 63.1 1.0
PG A:3PO203 2.9 62.6 1.0
PB A:3PO203 2.9 42.7 1.0
O3B A:3PO203 2.9 71.5 1.0
CG A:ASN163 3.1 39.0 1.0
O3A A:3PO203 3.1 65.3 1.0
O2G A:3PO203 3.2 53.9 1.0
HD22 A:ASN163 3.3 58.4 1.0
O1A A:3PO203 3.5 79.0 1.0
HH12 A:ARG137 3.5 33.7 1.0
ND2 A:ASN163 3.6 48.7 1.0
PA A:3PO203 3.9 74.8 1.0
N7 A:5AD202 4.0 36.7 1.0
NH1 A:ARG137 4.2 28.1 1.0
O A:ASN163 4.2 27.5 1.0
O1G A:3PO203 4.2 68.2 1.0
HA A:ASN163 4.2 40.3 1.0
O2A A:3PO203 4.3 58.6 1.0
O A:HOH302 4.3 49.3 1.0
O2B A:3PO203 4.3 49.9 1.0
H8 A:5AD202 4.3 43.9 1.0
HG A:SER166 4.4 34.3 1.0
OE1 A:GLU140 4.4 30.4 1.0
CB A:ASN163 4.4 31.5 1.0
HH11 A:ARG137 4.4 33.7 1.0
HD21 A:ASN163 4.5 58.4 1.0
C8 A:5AD202 4.5 36.6 1.0
OG A:SER166 4.6 28.5 1.0
OD2 A:ASP167 4.6 53.2 1.0
OE2 A:GLU140 4.6 33.4 1.0
CA A:ASN163 4.6 33.6 1.0
C A:ASN163 4.7 36.9 1.0
HB2 A:ASN163 4.7 37.8 1.0
OD1 A:ASP167 4.8 47.1 1.0
HH22 A:ARG137 4.8 38.3 1.0
CD A:GLU140 4.9 32.5 1.0

Reference:

R.Mascarenhas, M.Ruetz, L.Mcdevitt, M.Koutmos, R.Banerjee. Mobile Loop Dynamics in Adenosyltransferase Control Binding and Reactivity of Coenzyme B 12 . Proc.Natl.Acad.Sci.Usa V. 117 30412 2020.
ISSN: ESSN 1091-6490
PubMed: 33199623
DOI: 10.1073/PNAS.2007332117
Page generated: Mon Jan 25 15:17:33 2021

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy