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Nickel in PDB 1xu1: The Crystal Structure of April Bound to Taci

Protein crystallography data

The structure of The Crystal Structure of April Bound to Taci, PDB code: 1xu1 was solved by S.G.Hymowitz, D.R.Patel, H.J.A.Wallweber, S.Runyon, M.Yan, J.Yin, S.K.Shriver, N.C.Gordon, B.Pan, N.J.Skelton, R.F.Kelley, M.A.Starovasnik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.339, 91.839, 102.268, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 20.3

Nickel Binding Sites:

The binding sites of Nickel atom in the The Crystal Structure of April Bound to Taci (pdb code 1xu1). 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 The Crystal Structure of April Bound to Taci, PDB code: 1xu1:

Nickel binding site 1 out of 1 in 1xu1

Go back to Nickel Binding Sites List in 1xu1
Nickel binding site 1 out of 1 in the The Crystal Structure of April Bound to Taci


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of The Crystal Structure of April Bound to Taci within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni101

b:9.0
occ:1.00
NE2 B:HIS106 2.2 20.6 1.0
NE2 D:HIS106 2.2 24.2 1.0
NE2 A:HIS106 2.3 32.3 1.0
O D:HOH281 2.4 44.2 1.0
O A:HOH242 2.5 33.5 1.0
O D:HOH253 2.6 36.8 1.0
CE1 A:HIS106 2.9 39.5 1.0
CE1 B:HIS106 3.2 26.6 1.0
CE1 D:HIS106 3.2 24.8 1.0
CD2 B:HIS106 3.2 21.8 1.0
CD2 D:HIS106 3.2 23.5 1.0
CD2 A:HIS106 3.4 35.0 1.0
ND1 A:HIS106 4.1 40.7 1.0
ND1 B:HIS106 4.3 22.1 1.0
ND1 D:HIS106 4.3 21.6 1.0
CG B:HIS106 4.4 20.2 1.0
CG A:HIS106 4.4 28.1 1.0
CG D:HIS106 4.4 20.4 1.0
CG B:LYS105 4.9 39.7 1.0

Reference:

S.G.Hymowitz, D.R.Patel, H.J.A.Wallweber, S.Runyon, M.Yan, J.Yin, S.K.Shriver, N.C.Gordon, B.Pan, N.J.Skelton, R.F.Kelley, M.A.Starovasnik. Structures of April-Receptor Complexes: Like Bcma, Taci Employs Only A Single Cysteine-Rich Domain For High-Affinity Ligand Binding J.Biol.Chem. V. 280 7218 2005.
ISSN: ISSN 0021-9258
PubMed: 15542592
DOI: 10.1074/JBC.M411714200
Page generated: Wed Oct 9 16:33:07 2024

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