Atomistry » Magnesium » PDB 4c30-4cgk » 4cc7
Atomistry »
  Magnesium »
    PDB 4c30-4cgk »
      4cc7 »

Magnesium in PDB 4cc7: Crystal Structure of the Sixth or C-Terminal SH3 Domain of Human Tuba in Complex with Proline-Rich Peptides of N-Wasp. Space Group P41

Protein crystallography data

The structure of Crystal Structure of the Sixth or C-Terminal SH3 Domain of Human Tuba in Complex with Proline-Rich Peptides of N-Wasp. Space Group P41, PDB code: 4cc7 was solved by L.Polle, L.Rigano, R.Julian, K.Ireton, W.-D.Schubert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.59 / 1.97
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 88.570, 88.570, 69.730, 90.00, 90.00, 90.00
R / Rfree (%) 17.61 / 21.459

Other elements in 4cc7:

The structure of Crystal Structure of the Sixth or C-Terminal SH3 Domain of Human Tuba in Complex with Proline-Rich Peptides of N-Wasp. Space Group P41 also contains other interesting chemical elements:

Chlorine (Cl) 17 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Sixth or C-Terminal SH3 Domain of Human Tuba in Complex with Proline-Rich Peptides of N-Wasp. Space Group P41 (pdb code 4cc7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Sixth or C-Terminal SH3 Domain of Human Tuba in Complex with Proline-Rich Peptides of N-Wasp. Space Group P41, PDB code: 4cc7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4cc7

Go back to Magnesium Binding Sites List in 4cc7
Magnesium binding site 1 out of 2 in the Crystal Structure of the Sixth or C-Terminal SH3 Domain of Human Tuba in Complex with Proline-Rich Peptides of N-Wasp. Space Group P41


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 the Sixth or C-Terminal SH3 Domain of Human Tuba in Complex with Proline-Rich Peptides of N-Wasp. Space Group P41 within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Mg2577

b:48.1
occ:1.00
O K:PRO1529 2.3 31.1 1.0
O C:HOH2029 2.3 40.4 1.0
O C:HOH2030 2.5 45.6 1.0
O K:HOH2011 2.5 47.2 1.0
O K:HOH2026 2.6 42.8 0.5
O K:HOH2010 2.6 44.9 0.7
C K:PRO1529 3.5 30.9 1.0
NZ K:LYS1562 3.8 59.5 0.7
O K:HOH2008 4.0 38.4 1.0
O K:LYS1563 4.3 28.6 1.0
CA K:PRO1529 4.3 31.8 1.0
O K:GLU1531 4.4 23.0 1.0
N K:ASN1530 4.4 29.0 1.0
CA K:ASN1530 4.4 26.9 1.0
O C:VAL1548 4.7 27.9 1.0
O K:HOH2027 4.8 36.9 1.0
CA C:THR1549 4.8 29.2 1.0
CB K:PRO1529 4.8 37.1 1.0
C K:ASN1530 4.9 25.0 1.0

Magnesium binding site 2 out of 2 in 4cc7

Go back to Magnesium Binding Sites List in 4cc7
Magnesium binding site 2 out of 2 in the Crystal Structure of the Sixth or C-Terminal SH3 Domain of Human Tuba in Complex with Proline-Rich Peptides of N-Wasp. Space Group P41


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 the Sixth or C-Terminal SH3 Domain of Human Tuba in Complex with Proline-Rich Peptides of N-Wasp. Space Group P41 within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Mg2577

b:53.0
occ:1.00
O M:HOH2011 2.4 46.8 1.0
O M:PRO1529 2.5 34.4 1.0
O M:HOH2012 2.5 42.5 1.0
O M:HOH2013 3.2 52.1 1.0
NZ M:LYS1562 3.5 64.3 1.0
C M:PRO1529 3.6 34.5 1.0
CA M:PRO1529 4.1 34.0 1.0
O M:HOH2008 4.3 33.0 1.0
O M:LYS1563 4.4 34.3 1.0
CB M:PRO1529 4.4 37.6 1.0
O M:GLU1531 4.5 30.1 1.0
N M:ASN1530 4.7 33.6 1.0

Reference:

L.Polle, L.A.Rigano, R.Julian, K.Ireton, W.Schubert. Structural Details of Human Tuba Recruitment By Inlc of Listeria Monocytogenes Elucidate Bacterial Cell-Cell Spreading. Structure V. 22 304 2014.
ISSN: ISSN 0969-2126
PubMed: 24332715
DOI: 10.1016/J.STR.2013.10.017
Page generated: Thu Aug 15 16:46:04 2024

Last articles

Ca in 2PMY
Ca in 2PNY
Ca in 2PLY
Ca in 2PLX
Ca in 2PJP
Ca in 2PKT
Ca in 2PLT
Ca in 2PHX
Ca in 2PHW
Ca in 2PHU
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy