Praseodymium in PDB 2znr: Crystal Structure of the Dub Domain of Human Amsh-Lp

All present enzymatic activity of Crystal Structure of the Dub Domain of Human Amsh-Lp:
3.1.2.15;

The structure of Crystal Structure of the Dub Domain of Human Amsh-Lp, PDB code: 2znr was solved by Y.Sato, Y.Azusa, A.Yamagata, H.Mimura, X.Wang, M.Yamashita, K.Ookata, O.Nureki, K.Iwai, M.Komada, S.Fukai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.09 / 1.20
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	81.865, 81.865, 64.693, 90.00, 90.00, 120.00
R / Rfree (%)	14.9 / 16.5

The structure of Crystal Structure of the Dub Domain of Human Amsh-Lp also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Praseodymium atom in the Crystal Structure of the Dub Domain of Human Amsh-Lp (pdb code 2znr). This binding sites where shown within 5.0 Angstroms radius around Praseodymium atom.
In total only one binding site of Praseodymium was determined in the Crystal Structure of the Dub Domain of Human Amsh-Lp, PDB code: 2znr:

Praseodymium binding site 1 out of 1 in the Crystal Structure of the Dub Domain of Human Amsh-Lp


Mono view


Stereo pair view

A full contact list of Praseodymium with other atoms in the Pr binding site number 1 of Crystal Structure of the Dub Domain of Human Amsh-Lp within 5.0Å range: probe atom residue distance (Å) B Occ A:Pr437 b:21.2 occ:0.50 O A:HOH705 1.1 10.0 0.5 O A:HOH706 1.3 7.9 0.5 O A:HOH708 2.2 26.0 0.5 O A:HOH707 2.3 27.3 0.5 OD2 A:ASP274 2.5 13.3 0.5 OD1 A:ASP427 2.7 18.0 1.0 OD2 A:ASP427 2.7 19.2 1.0 OD1 A:ASP274 2.8 12.6 0.5 CG A:ASP274 3.0 10.6 0.5 CG A:ASP427 3.0 16.0 1.0 CB A:ASP274 4.5 10.2 0.5 CB A:ASP274 4.5 11.0 0.5 CB A:ASP427 4.5 14.1 1.0 O A:HOH468 4.6 11.9 1.0 CG A:ASP274 4.7 13.0 0.5 OD1 A:ASP274 4.8 14.7 0.5 O A:HOH650 4.9 38.4 1.0 OE1 A:GLU273 5.0 21.1 1.0

Y.Sato, A.Yoshikawa, A.Yamagata, H.Mimura, M.Yamashita, K.Ookata, O.Nureki, K.Iwai, M.Komada, S.Fukai. Structural Basis For Specific Cleavage of Lys 63-Linked Polyubiquitin Chains Nature V. 455 358 2008.
ISSN: ISSN 0028-0836
PubMed: 18758443
DOI: 10.1038/NATURE07254