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Sodium in PDB 1g1s: P-Selectin Lectin/Egf Domains Complexed with Psgl-1 Peptide

Protein crystallography data

The structure of P-Selectin Lectin/Egf Domains Complexed with Psgl-1 Peptide, PDB code: 1g1s was solved by W.S.Somers, R.T.Camphausen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.90
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 63.445, 96.756, 187.289, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 23.5

Other elements in 1g1s:

The structure of P-Selectin Lectin/Egf Domains Complexed with Psgl-1 Peptide also contains other interesting chemical elements:

Strontium (Sr) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the P-Selectin Lectin/Egf Domains Complexed with Psgl-1 Peptide (pdb code 1g1s). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the P-Selectin Lectin/Egf Domains Complexed with Psgl-1 Peptide, PDB code: 1g1s:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 1g1s

Go back to Sodium Binding Sites List in 1g1s
Sodium binding site 1 out of 2 in the P-Selectin Lectin/Egf Domains Complexed with Psgl-1 Peptide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of P-Selectin Lectin/Egf Domains Complexed with Psgl-1 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na903

b:33.5
occ:1.00
O B:HOH954 2.4 47.6 1.0
NZ B:LYS112 3.9 43.1 1.0
OD2 C:ASP609 4.3 36.4 1.0
O C:HOH55 4.5 39.5 1.0
O C:HOH200 4.7 55.0 1.0
CE B:LYS112 4.9 43.6 1.0

Sodium binding site 2 out of 2 in 1g1s

Go back to Sodium Binding Sites List in 1g1s
Sodium binding site 2 out of 2 in the P-Selectin Lectin/Egf Domains Complexed with Psgl-1 Peptide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of P-Selectin Lectin/Egf Domains Complexed with Psgl-1 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Na904

b:36.3
occ:1.00
O C:HOH199 2.2 45.8 1.0
O C:HOH55 2.2 39.5 1.0
OD2 C:ASP609 2.4 36.4 1.0
O C:HOH185 2.4 52.3 1.0
OD1 C:ASP609 2.5 35.7 1.0
O C:HOH200 2.5 55.0 1.0
OD2 C:ASP611 2.7 46.8 1.0
CG C:ASP609 2.7 39.0 1.0
CG C:ASP611 3.5 43.5 1.0
CB C:ASP611 3.9 34.9 1.0
CB C:ASP609 4.2 32.4 1.0
OD1 C:ASP611 4.3 41.2 1.0
CE1 C:PHE612 4.7 32.0 1.0
O C:HOH175 4.7 52.7 1.0
N C:ASP611 4.9 36.7 1.0
O C:HOH159 4.9 53.3 1.0
CA C:ASP609 4.9 36.0 1.0

Reference:

W.S.Somers, J.Tang, G.D.Shaw, R.T.Camphausen. Insights Into the Molecular Basis of Leukocyte Tethering and Rolling Revealed By Structures of P- and E-Selectin Bound to Sle(X) and Psgl-1. Cell(Cambridge,Mass.) V. 103 467 2000.
ISSN: ISSN 0092-8674
PubMed: 11081633
DOI: 10.1016/S0092-8674(00)00138-0
Page generated: Tue Dec 15 05:23:57 2020

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