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Zinc in PDB 1taz: Catalytic Domain of Human Phosphodiesterase 1B

Enzymatic activity of Catalytic Domain of Human Phosphodiesterase 1B

All present enzymatic activity of Catalytic Domain of Human Phosphodiesterase 1B:
3.1.4.17;

Protein crystallography data

The structure of Catalytic Domain of Human Phosphodiesterase 1B, PDB code: 1taz was solved by K.Y.J.Zhang, G.L.Card, Y.Suzuki, D.R.Artis, D.Fong, S.Gillette, D.Hsieh, J.Neiman, B.L.West, C.Zhang, M.V.Milburn, S.-H.Kim, J.Schlessinger, G.Bollag, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.55 / 1.77
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 87.232, 87.232, 134.151, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 19.3

Other elements in 1taz:

The structure of Catalytic Domain of Human Phosphodiesterase 1B also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Catalytic Domain of Human Phosphodiesterase 1B (pdb code 1taz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Catalytic Domain of Human Phosphodiesterase 1B, PDB code: 1taz:

Zinc binding site 1 out of 1 in 1taz

Go back to Zinc Binding Sites List in 1taz
Zinc binding site 1 out of 1 in the Catalytic Domain of Human Phosphodiesterase 1B


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Catalytic Domain of Human Phosphodiesterase 1B within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:22.1
occ:1.00
OD1 A:ASP370 2.1 17.4 1.0
OD2 A:ASP264 2.1 17.1 1.0
O A:HOH1007 2.1 16.1 1.0
NE2 A:HIS263 2.2 16.4 1.0
NE2 A:HIS227 2.2 17.0 1.0
O A:HOH1008 2.4 21.7 1.0
CD2 A:HIS263 3.0 16.5 1.0
CG A:ASP370 3.1 19.3 1.0
CG A:ASP264 3.1 17.1 1.0
CD2 A:HIS227 3.1 18.1 1.0
CE1 A:HIS227 3.2 18.1 1.0
CE1 A:HIS263 3.2 16.5 1.0
OD2 A:ASP370 3.3 22.4 1.0
OD1 A:ASP264 3.6 15.2 1.0
MG A:MG1002 3.8 17.6 1.0
O A:HOH1006 4.1 17.9 1.0
O A:HOH1009 4.2 20.5 1.0
CG A:HIS263 4.2 15.8 1.0
ND1 A:HIS263 4.3 16.2 1.0
CD2 A:HIS223 4.3 19.0 1.0
CG A:HIS227 4.3 16.1 1.0
ND1 A:HIS227 4.3 17.4 1.0
CB A:ASP264 4.3 16.2 1.0
CB A:ASP370 4.4 17.6 1.0
NE2 A:HIS223 4.5 19.9 1.0
O A:HOH1004 4.7 16.0 1.0
O A:HOH1068 4.7 38.0 1.0
CG2 A:VAL231 4.8 17.1 1.0
CA A:ASP370 4.9 17.5 1.0
O A:ASP370 4.9 18.5 1.0

Reference:

K.Y.J.Zhang, G.L.Card, Y.Suzuki, D.R.Artis, D.Fong, S.Gillette, D.Hsieh, J.Neiman, B.L.West, C.Zhang, M.V.Milburn, S.-H.Kim, J.Schlessinger, G.Bollag. A Glutamine Switch Mechanism For Nucleotide Selectivity By Phosphodiesterases Mol.Cell V. 15 279 2004.
ISSN: ISSN 1097-2765
PubMed: 15260978
DOI: 10.1016/J.MOLCEL.2004.07.005
Page generated: Mon Jan 25 16:13:53 2021

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