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Nickel in PDB 1elr: Crystal Structure of the TPR2A Domain of Hop in Complex with the HSP90 Peptide Meevd

Protein crystallography data

The structure of Crystal Structure of the TPR2A Domain of Hop in Complex with the HSP90 Peptide Meevd, PDB code: 1elr was solved by C.Scheufler, A.Brinker, F.U.Hartl, I.Moarefi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 9.93 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 73.280, 48.270, 38.060, 90.00, 91.30, 90.00
R / Rfree (%) 18.1 / 21.9

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of the TPR2A Domain of Hop in Complex with the HSP90 Peptide Meevd (pdb code 1elr). 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 Crystal Structure of the TPR2A Domain of Hop in Complex with the HSP90 Peptide Meevd, PDB code: 1elr:

Nickel binding site 1 out of 1 in 1elr

Go back to Nickel Binding Sites List in 1elr
Nickel binding site 1 out of 1 in the Crystal Structure of the TPR2A Domain of Hop in Complex with the HSP90 Peptide Meevd


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of the TPR2A Domain of Hop in Complex with the HSP90 Peptide Meevd within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni200

b:15.1
occ:1.00
NE2 A:HIS247 2.3 11.1 1.0
O A:HOH14 2.4 13.4 1.0
O A:HOH60 2.4 18.9 1.0
O A:HOH59 2.4 17.3 1.0
CD2 A:HIS247 3.2 10.2 1.0
CE1 A:HIS247 3.3 8.3 1.0
O A:HOH43 4.1 20.9 1.0
O A:HOH111 4.2 40.1 1.0
ND1 A:HIS247 4.3 10.3 1.0
CG A:HIS247 4.4 8.5 1.0
CG2 A:THR243 4.7 12.5 1.0

Reference:

C.Scheufler, A.Brinker, G.Bourenkov, S.Pegoraro, L.Moroder, H.Bartunik, F.U.Hartl, I.Moarefi. Structure of Tpr Domain-Peptide Complexes: Critical Elements in the Assembly of the HSP70-HSP90 Multichaperone Machine. Cell(Cambridge,Mass.) V. 101 199 2000.
ISSN: ISSN 0092-8674
PubMed: 10786835
DOI: 10.1016/S0092-8674(00)80830-2
Page generated: Fri Sep 25 07:52:00 2020
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