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Yttrium in PDB 2ahx: Crystal Structure of ERBB4/HER4 Extracellular Domain

Enzymatic activity of Crystal Structure of ERBB4/HER4 Extracellular Domain

All present enzymatic activity of Crystal Structure of ERBB4/HER4 Extracellular Domain:
2.7.1.112;

Protein crystallography data

The structure of Crystal Structure of ERBB4/HER4 Extracellular Domain, PDB code: 2ahx was solved by S.Bouyain, P.A.Longo, S.Li, K.M.Ferguson, D.J.Leahy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.88 / 2.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 76.960, 203.090, 261.320, 90.00, 90.00, 90.00
R / Rfree (%) 23.5 / 26.5

Yttrium Binding Sites:

The binding sites of Yttrium atom in the Crystal Structure of ERBB4/HER4 Extracellular Domain (pdb code 2ahx). This binding sites where shown within 5.0 Angstroms radius around Yttrium atom.
In total only one binding site of Yttrium was determined in the Crystal Structure of ERBB4/HER4 Extracellular Domain, PDB code: 2ahx:

Yttrium binding site 1 out of 1 in 2ahx

Go back to Yttrium Binding Sites List in 2ahx
Yttrium binding site 1 out of 1 in the Crystal Structure of ERBB4/HER4 Extracellular Domain


Mono view


Stereo pair view

A full contact list of Yttrium with other atoms in the Y binding site number 1 of Crystal Structure of ERBB4/HER4 Extracellular Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Y3001

b:38.7
occ:0.50
OE1 B:GLU588 1.7 38.6 1.0
OD2 B:ASP586 2.4 17.5 1.0
OD1 B:ASP586 2.5 20.0 1.0
CG B:ASP586 2.8 20.8 1.0
OD2 B:ASP584 2.8 28.9 1.0
CD B:GLU588 2.9 28.1 1.0
CG B:ASP584 3.4 23.8 1.0
OD1 B:ASP584 3.7 18.3 1.0
OE2 B:GLU588 3.8 32.0 1.0
CG B:GLU588 3.8 24.2 1.0
CB B:GLU588 4.1 22.4 1.0
CB B:ASP586 4.3 17.6 1.0
NE2 B:HIS590 4.4 20.4 1.0
CB B:ASP584 4.5 14.3 1.0
CE1 B:HIS590 4.9 17.5 1.0

Reference:

S.Bouyain, P.A.Longo, S.Li, K.M.Ferguson, D.J.Leahy. The Extracellular Region of ERBB4 Adopts A Tethered Conformation in the Absence of Ligand Proc.Natl.Acad.Sci.Usa V. 102 15024 2005.
ISSN: ISSN 0027-8424
PubMed: 16203964
DOI: 10.1073/PNAS.0507591102
Page generated: Wed Dec 16 02:40:50 2020

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