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Nickel in PDB 3lei: Lectin Domain of Lectinolysin Complexed with Fucose

Protein crystallography data

The structure of Lectin Domain of Lectinolysin Complexed with Fucose, PDB code: 3lei was solved by S.C.Feil, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.64 / 1.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 67.010, 67.010, 97.800, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 24.7

Other elements in 3lei:

The structure of Lectin Domain of Lectinolysin Complexed with Fucose also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Nickel Binding Sites:

The binding sites of Nickel atom in the Lectin Domain of Lectinolysin Complexed with Fucose (pdb code 3lei). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Lectin Domain of Lectinolysin Complexed with Fucose, PDB code: 3lei:

Nickel binding site 1 out of 1 in 3lei

Go back to Nickel Binding Sites List in 3lei
Nickel binding site 1 out of 1 in the Lectin Domain of Lectinolysin Complexed with Fucose


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Lectin Domain of Lectinolysin Complexed with Fucose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni191

b:15.9
occ:0.35
O A:HOH296 1.9 25.3 1.0
O A:HOH295 2.0 16.5 1.0
O A:HOH294 2.0 22.1 1.0
O A:HOH298 2.1 19.6 1.0
NE2 A:HIS80 2.2 17.6 1.0
O A:HOH297 2.2 20.8 1.0
CE1 A:HIS80 3.1 19.1 1.0
CD2 A:HIS80 3.2 17.0 1.0
O A:HOH299 4.2 26.8 1.0
ND1 A:HIS80 4.2 18.9 1.0
O A:HOH220 4.3 30.7 1.0
CG A:HIS80 4.3 19.1 1.0
OD1 A:ASP77 4.4 23.7 1.0

Reference:

S.C.Feil, S.Lawrence, T.D.Mulhern, J.K.Holien, E.M.Hotze, S.Farrand, R.K.Tweten, M.W.Parker. Structure of the Lectin Regulatory Domain of the Cholesterol-Dependent Cytolysin Lectinolysin Reveals the Basis For Its Lewis Antigen Specificity. Structure V. 20 248 2012.
ISSN: ISSN 0969-2126
PubMed: 22325774
DOI: 10.1016/J.STR.2011.11.017
Page generated: Wed Oct 9 17:29:41 2024

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