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Caesium in PDB 5a9h: Crystal Structure of the Extracellular Domain of PEPT2

Protein crystallography data

The structure of Crystal Structure of the Extracellular Domain of PEPT2, PDB code: 5a9h was solved by J.H.Beale, S.Newstead, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.46 / 2.06
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 43.070, 43.070, 220.530, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 23.3

Caesium Binding Sites:

The binding sites of Caesium atom in the Crystal Structure of the Extracellular Domain of PEPT2 (pdb code 5a9h). This binding sites where shown within 5.0 Angstroms radius around Caesium atom.
In total 2 binding sites of Caesium where determined in the Crystal Structure of the Extracellular Domain of PEPT2, PDB code: 5a9h:
Jump to Caesium binding site number: 1; 2;

Caesium binding site 1 out of 2 in 5a9h

Go back to Caesium Binding Sites List in 5a9h
Caesium binding site 1 out of 2 in the Crystal Structure of the Extracellular Domain of PEPT2


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 1 of Crystal Structure of the Extracellular Domain of PEPT2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cs1603

b:35.0
occ:0.27
ND1 A:HIS451 1.9 35.1 0.5
CE1 A:HIS451 2.3 27.1 0.5
ND1 A:HIS451 2.3 28.9 0.5
CG A:HIS451 2.4 26.7 0.5
NE2 A:HIS451 2.4 26.1 0.5
CD2 A:HIS451 2.5 26.3 0.5
O A:HOH2093 2.6 69.9 1.0
CE1 A:HIS451 2.8 35.9 0.5
CG A:HIS451 2.9 33.0 0.5
CB A:HIS451 3.3 28.7 0.5
CB A:HIS451 3.4 24.9 0.5
NE2 A:HIS451 4.0 36.8 0.5
CD2 A:HIS451 4.0 35.9 0.5
O A:HOH2026 4.4 52.3 1.0
CA A:HIS451 4.7 27.5 0.5
CA A:HIS451 4.7 24.7 0.5
OD1 A:ASN448 5.0 41.7 1.0

Caesium binding site 2 out of 2 in 5a9h

Go back to Caesium Binding Sites List in 5a9h
Caesium binding site 2 out of 2 in the Crystal Structure of the Extracellular Domain of PEPT2


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 2 of Crystal Structure of the Extracellular Domain of PEPT2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cs1605

b:49.2
occ:0.60
NE2 A:HIS476 1.7 43.6 1.0
ND1 A:HIS465 2.2 46.3 1.0
CE1 A:HIS476 2.5 45.4 1.0
OD2 A:ASP478 2.5 63.9 1.0
OD1 A:ASP478 2.5 48.6 1.0
CG A:ASP478 2.8 52.3 1.0
CD2 A:HIS476 3.0 43.0 1.0
CE1 A:HIS465 3.1 47.8 1.0
CG A:HIS465 3.3 42.0 1.0
CB A:HIS465 3.7 36.0 1.0
ND1 A:HIS476 3.7 46.5 1.0
CG A:HIS476 3.9 42.5 1.0
O A:HOH2030 4.0 47.5 1.0
NE2 A:HIS465 4.3 46.9 1.0
CB A:ASP478 4.3 42.8 1.0
CA A:HIS465 4.4 34.7 1.0
CD2 A:HIS465 4.4 44.6 1.0

Reference:

J.H.Beale, J.L.Parker, F.Samsudin, A.L.Barrett, A.Senan, L.E.Bird, D.Scott, R.J.Owens, M.S.P.Sanson, S.J.Tucker, D.Meredith, P.W.Fowler, S.Newstead. Crystal Structures of the Extracellular Domain From PEPT1 and PEPT2 Provide Novel Insights Into Mammalian Peptide Transport Structure V. 23 1889 2015.
ISSN: ISSN 0969-2126
PubMed: 26320580
DOI: 10.1016/J.STR.2015.07.016
Page generated: Sun Dec 13 10:56:40 2020

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