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Chlorine in PDB 3vko: Galectin-8 N-Terminal Domain in Complex with Sialyllactosamine

Protein crystallography data

The structure of Galectin-8 N-Terminal Domain in Complex with Sialyllactosamine, PDB code: 3vko was solved by S.Kamitori, H.Yoshida, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.60 / 2.08
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.710, 61.500, 84.070, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 24.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Galectin-8 N-Terminal Domain in Complex with Sialyllactosamine (pdb code 3vko). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Galectin-8 N-Terminal Domain in Complex with Sialyllactosamine, PDB code: 3vko:

Chlorine binding site 1 out of 1 in 3vko

Go back to Chlorine Binding Sites List in 3vko
Chlorine binding site 1 out of 1 in the Galectin-8 N-Terminal Domain in Complex with Sialyllactosamine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Galectin-8 N-Terminal Domain in Complex with Sialyllactosamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl204

b:47.0
occ:1.00
O A:HOH420 2.8 94.9 1.0
N A:ASP112 3.0 38.1 1.0
O A:HOH401 3.2 91.6 1.0
CB A:ASP112 3.6 43.9 1.0
N A:LYS111 3.7 38.8 1.0
CB A:LYS111 3.8 41.6 1.0
CA A:ASP112 3.8 39.7 1.0
CB A:LEU110 3.8 34.9 1.0
OD1 A:ASP112 3.8 51.5 1.0
C A:LYS111 3.9 38.6 1.0
CA A:LYS111 4.0 38.8 1.0
CG A:ASP112 4.0 48.3 1.0
N A:LYS113 4.3 37.8 1.0
CD1 A:LEU110 4.4 35.5 1.0
C A:ASP112 4.4 38.8 1.0
C A:LEU110 4.4 37.8 1.0
CE A:LYS113 4.5 49.4 1.0
CG A:LYS113 4.5 40.2 1.0
CG A:LYS111 4.7 41.9 1.0
CG A:LEU110 4.7 36.4 1.0
CA A:LEU110 4.7 36.4 1.0
CD A:LYS113 4.8 45.1 1.0

Reference:

H.Yoshida, S.Yamashita, M.Teraoka, A.Itoh, S.Nakakita, N.Nishi, S.Kamitori. X-Ray Structure of A Protease-Resistant Mutant Form of Human Galectin-8 with Two Carbohydrate Recognition Domains Febs J. V. 279 3937 2012.
ISSN: ISSN 1742-464X
PubMed: 22913484
DOI: 10.1111/J.1742-4658.2012.08753.X
Page generated: Sun Jul 21 07:01:14 2024

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