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Chlorine in PDB 4ah4: Crystal Structure of Fucose Binding Lectin From Aspergillus Fumigatus (Afl) in Complex with Bga Oligosaccharide.

Protein crystallography data

The structure of Crystal Structure of Fucose Binding Lectin From Aspergillus Fumigatus (Afl) in Complex with Bga Oligosaccharide., PDB code: 4ah4 was solved by J.Houser, J.Komarek, N.Kostlanova, M.Lahmann, G.Cioci, A.Varrot, A.Imberty, M.Wimmerova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 77.15 / 1.75
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 46.420, 47.440, 80.086, 103.61, 91.96, 113.08
R / Rfree (%) 16.758 / 21.075

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Fucose Binding Lectin From Aspergillus Fumigatus (Afl) in Complex with Bga Oligosaccharide. (pdb code 4ah4). 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 Crystal Structure of Fucose Binding Lectin From Aspergillus Fumigatus (Afl) in Complex with Bga Oligosaccharide., PDB code: 4ah4:

Chlorine binding site 1 out of 1 in 4ah4

Go back to Chlorine Binding Sites List in 4ah4
Chlorine binding site 1 out of 1 in the Crystal Structure of Fucose Binding Lectin From Aspergillus Fumigatus (Afl) in Complex with Bga Oligosaccharide.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Fucose Binding Lectin From Aspergillus Fumigatus (Afl) in Complex with Bga Oligosaccharide. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1000

b:35.7
occ:1.00
NZ A:LYS50 3.1 34.3 1.0
CE A:LYS50 3.2 32.1 1.0
CD A:LYS50 4.5 33.9 1.0

Reference:

J.Houser, J.Komarek, G.Cioci, A.Varrot, A.Imberty, M.Wimmerova. Structural Insights Into Aspergillus Fumigatus Lectin Specificity: Afl Binding Sites Are Functionally Non-Equivalent Acta Crystallogr.,Sect.D V. 71 442 2015.
ISSN: ISSN 0907-4449
PubMed: 25760594
DOI: 10.1107/S1399004714026595
Page generated: Sat Dec 12 10:23:25 2020

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