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Nickel in PDB 1xu2: The Crystal Structure of April Bound to Bcma

Protein crystallography data

The structure of The Crystal Structure of April Bound to Bcma, PDB code: 1xu2 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 / 2.35
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 114.294, 114.294, 91.180, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 21.3

Nickel Binding Sites:

The binding sites of Nickel atom in the The Crystal Structure of April Bound to Bcma (pdb code 1xu2). 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 Bcma, PDB code: 1xu2:

Nickel binding site 1 out of 1 in 1xu2

Go back to Nickel Binding Sites List in 1xu2
Nickel binding site 1 out of 1 in the The Crystal Structure of April Bound to Bcma


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 Bcma within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ni301

b:58.6
occ:1.00
NE2 B:HIS106 2.2 56.5 1.0
NE2 D:HIS106 2.3 62.2 1.0
NE2 A:HIS106 2.6 53.4 1.0
CE1 A:HIS106 2.6 54.2 1.0
CE1 B:HIS106 3.0 56.6 1.0
CD2 D:HIS106 3.1 60.9 1.0
CD2 B:HIS106 3.3 55.2 1.0
CE1 D:HIS106 3.5 62.0 1.0
ND1 A:HIS106 3.8 54.5 1.0
CD2 A:HIS106 3.8 51.0 1.0
ND1 B:HIS106 4.2 55.6 1.0
CG D:HIS106 4.3 60.1 1.0
CG B:HIS106 4.3 54.2 1.0
CG A:HIS106 4.4 45.9 1.0
ND1 D:HIS106 4.5 60.4 1.0
NZ B:LYS105 4.9 55.9 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: Fri Sep 25 08:04:14 2020
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