Atomistry » Magnesium » PDB 3hx0-3i5x » 3hxx
Atomistry »
  Magnesium »
    PDB 3hx0-3i5x »
      3hxx »

Magnesium in PDB 3hxx: Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp

Enzymatic activity of Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp

All present enzymatic activity of Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp:
6.1.1.7;

Protein crystallography data

The structure of Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp, PDB code: 3hxx was solved by M.Guo, X.-L.Yang, P.Schimmel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.10 / 2.11
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.823, 111.393, 118.538, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 23.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp (pdb code 3hxx). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp, PDB code: 3hxx:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 3hxx

Go back to Magnesium Binding Sites List in 3hxx
Magnesium binding site 1 out of 3 in the Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg443

b:17.5
occ:1.00
O A:HOH470 1.9 17.7 1.0
O2G A:ACP442 2.0 18.5 1.0
O A:HOH613 2.0 21.9 1.0
O1B A:ACP442 2.1 16.4 1.0
O A:HOH476 2.2 16.0 1.0
O A:HOH482 2.3 15.4 1.0
PG A:ACP442 3.3 16.0 1.0
PB A:ACP442 3.3 17.0 1.0
C3B A:ACP442 3.7 8.3 1.0
O3G A:ACP442 3.9 26.3 1.0
NE2 A:HIS86 4.0 13.8 1.0
NH1 A:ARG69 4.1 9.1 1.0
OD2 A:ASP76 4.1 19.0 1.0
OD1 A:ASP76 4.1 19.9 1.0
O A:HOH818 4.2 45.0 1.0
O2B A:ACP442 4.3 25.0 1.0
O A:HOH571 4.4 29.6 1.0
O3A A:ACP442 4.4 21.2 1.0
O A:HOH692 4.5 32.9 1.0
O1G A:ACP442 4.5 19.0 1.0
CD2 A:HIS86 4.5 12.7 1.0
N7 A:ACP442 4.6 15.2 1.0
CG A:ASP76 4.6 10.2 1.0
ND1 A:HIS74 4.8 40.0 1.0
O A:HOH616 4.8 20.3 1.0
O A:HOH751 5.0 45.9 1.0

Magnesium binding site 2 out of 3 in 3hxx

Go back to Magnesium Binding Sites List in 3hxx
Magnesium binding site 2 out of 3 in the Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg444

b:20.8
occ:1.00
O2B A:ACP442 2.2 25.0 1.0
O2A A:ACP442 2.2 16.8 1.0
OE2 A:GLU183 2.3 33.3 1.0
OE1 A:GLU209 2.4 18.9 1.0
O A:HOH480 2.5 30.9 1.0
O A:HOH469 2.7 22.6 1.0
MG A:MG445 3.1 33.7 1.0
CD A:GLU209 3.2 17.8 1.0
CD A:GLU183 3.3 18.5 1.0
OE2 A:GLU209 3.3 23.3 1.0
PA A:ACP442 3.3 18.3 1.0
PB A:ACP442 3.4 17.0 1.0
O3A A:ACP442 3.5 21.2 1.0
OE1 A:GLU183 3.6 28.4 1.0
ND2 A:ASN212 3.6 18.0 1.0
CG A:ASN212 4.0 27.9 1.0
O A:HOH616 4.1 20.3 1.0
CB A:ASN212 4.1 13.4 1.0
O1A A:ACP442 4.2 20.7 1.0
C3B A:ACP442 4.3 8.3 1.0
O A:HOH512 4.4 30.3 1.0
O A:ASP167 4.4 26.0 1.0
O A:HOH692 4.5 32.9 1.0
CD1 A:TRP170 4.6 38.6 1.0
CG A:GLU183 4.6 15.2 1.0
O1B A:ACP442 4.6 16.4 1.0
CG A:GLU209 4.6 12.0 1.0
O5' A:ACP442 4.6 13.7 1.0
O3' A:ACP442 4.7 17.6 1.0
OD1 A:ASN212 4.8 25.5 1.0
NE1 A:TRP170 4.9 37.7 1.0
C5' A:ACP442 4.9 20.7 1.0
C3' A:ACP442 4.9 13.7 1.0

Magnesium binding site 3 out of 3 in 3hxx

Go back to Magnesium Binding Sites List in 3hxx
Magnesium binding site 3 out of 3 in the Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Catalytic Fragment of E. Coli Alars in Complex with Amppcp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg445

b:33.7
occ:1.00
O A:HOH616 2.0 20.3 1.0
O A:HOH469 2.0 22.6 1.0
O2B A:ACP442 2.1 25.0 1.0
OE2 A:GLU209 2.1 23.3 1.0
O A:HOH481 2.2 23.8 1.0
O3G A:ACP442 2.4 26.3 1.0
MG A:MG444 3.1 20.8 1.0
CD A:GLU209 3.2 17.8 1.0
PB A:ACP442 3.2 17.0 1.0
C3B A:ACP442 3.3 8.3 1.0
PG A:ACP442 3.5 16.0 1.0
OE1 A:GLU209 3.5 18.9 1.0
O A:HOH636 3.7 33.6 1.0
OE1 A:GLU183 4.0 28.4 1.0
O1B A:ACP442 4.1 16.4 1.0
O A:HOH482 4.2 15.4 1.0
O3A A:ACP442 4.5 21.2 1.0
OE2 A:GLU183 4.5 33.3 1.0
O A:HOH692 4.5 32.9 1.0
O2G A:ACP442 4.5 18.5 1.0
O1G A:ACP442 4.5 19.0 1.0
CG A:GLU209 4.5 12.0 1.0
O A:HOH480 4.5 30.9 1.0
OD1 A:ASP167 4.6 38.9 1.0
CD A:GLU183 4.7 18.5 1.0
O A:HOH485 4.7 27.9 1.0
CB A:GLU209 4.8 11.5 1.0
O2A A:ACP442 4.8 16.8 1.0
CG A:ASP167 4.9 47.0 1.0

Reference:

M.Guo, Y.E.Chong, R.Shapiro, K.Beebe, X.L.Yang, P.Schimmel. Paradox of Mistranslation of Serine For Alanine Caused By Alars Recognition Dilemma. Nature V. 462 808 2009.
ISSN: ISSN 0028-0836
PubMed: 20010690
DOI: 10.1038/NATURE08612
Page generated: Mon Dec 14 08:15:05 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy