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Magnesium in PDB 3jvv: Crystal Structure of P. Aeruginosa Pilt with Bound Amp-Pcp

Protein crystallography data

The structure of Crystal Structure of P. Aeruginosa Pilt with Bound Amp-Pcp, PDB code: 3jvv was solved by A.M.Misic, K.A.Satyshur, K.T.Forest, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.12 / 2.60
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 108.483, 119.552, 185.535, 90.00, 90.00, 90.00
R / Rfree (%) 24.4 / 29.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of P. Aeruginosa Pilt with Bound Amp-Pcp (pdb code 3jvv). 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 P. Aeruginosa Pilt with Bound Amp-Pcp, PDB code: 3jvv:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 3jvv

Go back to Magnesium Binding Sites List in 3jvv
Magnesium binding site 1 out of 3 in the Crystal Structure of P. Aeruginosa Pilt with Bound Amp-Pcp


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 P. Aeruginosa Pilt with Bound Amp-Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:55.7
occ:1.00
O2G A:ACP400 1.8 68.8 1.0
O1B A:ACP400 2.4 68.4 1.0
OG A:SER137 2.7 51.6 1.0
PG A:ACP400 3.0 68.5 1.0
C3B A:ACP400 3.1 68.3 1.0
OE2 A:GLU163 3.1 66.6 1.0
PB A:ACP400 3.2 68.3 1.0
CB A:SER137 3.4 51.9 1.0
N A:SER137 4.0 50.5 1.0
CD A:GLU163 4.0 65.7 1.0
O1G A:ACP400 4.0 67.4 1.0
O3G A:ACP400 4.0 68.0 1.0
OE1 A:GLU163 4.1 67.2 1.0
O2B A:ACP400 4.1 68.3 1.0
O1A A:ACP400 4.1 68.9 1.0
CA A:SER137 4.3 50.6 1.0
O3A A:ACP400 4.5 68.6 1.0
O2A A:ACP400 4.6 68.4 1.0
PA A:ACP400 4.7 68.1 1.0
CB A:LYS136 5.0 51.1 1.0
CE A:LYS136 5.0 51.8 1.0

Magnesium binding site 2 out of 3 in 3jvv

Go back to Magnesium Binding Sites List in 3jvv
Magnesium binding site 2 out of 3 in the Crystal Structure of P. Aeruginosa Pilt with Bound Amp-Pcp


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 P. Aeruginosa Pilt with Bound Amp-Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:44.0
occ:1.00
O B:HOH362 1.9 35.0 1.0
C3B B:ACP400 2.1 59.2 1.0
OG B:SER137 2.4 40.6 1.0
O1B B:ACP400 2.8 59.1 1.0
O2G B:ACP400 2.9 59.7 1.0
PG B:ACP400 3.0 58.8 1.0
PB B:ACP400 3.0 58.5 1.0
OE2 B:GLU163 3.0 55.9 1.0
OE1 B:GLU163 3.0 55.5 1.0
O1A B:ACP400 3.2 59.4 1.0
CB B:SER137 3.3 41.1 1.0
O3G B:ACP400 3.4 58.7 1.0
CD B:GLU163 3.4 53.9 1.0
PA B:ACP400 4.0 60.0 1.0
O3A B:ACP400 4.0 59.6 1.0
NH2 B:ARG82 4.0 67.5 1.0
O2B B:ACP400 4.2 60.1 1.0
NH1 B:ARG82 4.2 66.0 1.0
N B:SER137 4.2 42.9 1.0
O2A B:ACP400 4.3 59.2 1.0
O1G B:ACP400 4.3 59.4 1.0
CA B:SER137 4.4 41.8 1.0
CZ B:ARG82 4.6 66.5 1.0
CG B:GLU163 4.9 51.9 1.0

Magnesium binding site 3 out of 3 in 3jvv

Go back to Magnesium Binding Sites List in 3jvv
Magnesium binding site 3 out of 3 in the Crystal Structure of P. Aeruginosa Pilt with Bound Amp-Pcp


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 P. Aeruginosa Pilt with Bound Amp-Pcp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg401

b:64.7
occ:1.00
C3B C:ACP400 2.5 69.9 1.0
OG C:SER137 2.6 51.5 1.0
CB C:SER137 2.8 50.2 1.0
O1B C:ACP400 2.8 68.9 1.0
OE2 C:GLU163 3.0 60.4 1.0
PB C:ACP400 3.3 69.0 1.0
OE1 C:GLU163 3.4 59.7 1.0
CD C:GLU163 3.6 59.6 1.0
PG C:ACP400 3.6 70.4 1.0
O1A C:ACP400 3.6 70.8 1.0
O2G C:ACP400 3.7 70.1 1.0
O1G C:ACP400 3.8 70.6 1.0
CA C:SER137 3.9 49.8 1.0
N C:SER137 4.0 49.8 1.0
O3A C:ACP400 4.2 70.1 1.0
PA C:ACP400 4.3 70.8 1.0
O2B C:ACP400 4.5 69.1 1.0
O2A C:ACP400 4.5 69.7 1.0
O C:HOH375 4.9 63.1 1.0
O3G C:ACP400 5.0 70.4 1.0

Reference:

A.M.Misic, K.A.Satyshur, K.T.Forest. P. Aeruginosa Pilt Structures with and Without Nucleotide Reveal A Dynamic Type IV Pilus Retraction Motor. J.Mol.Biol. V. 400 1011 2010.
ISSN: ISSN 0022-2836
PubMed: 20595000
DOI: 10.1016/J.JMB.2010.05.066
Page generated: Mon Dec 14 08:20:41 2020

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