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Zinc in PDB 1t9r: Catalytic Domain of Human Phosphodiesterase 5A

Enzymatic activity of Catalytic Domain of Human Phosphodiesterase 5A

All present enzymatic activity of Catalytic Domain of Human Phosphodiesterase 5A:
3.1.4.17;

Protein crystallography data

The structure of Catalytic Domain of Human Phosphodiesterase 5A, PDB code: 1t9r 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) 84.51 / 2.10
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 96.411, 96.411, 79.026, 90.00, 90.00, 120.00
R / Rfree (%) 20.2 / 24.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Catalytic Domain of Human Phosphodiesterase 5A (pdb code 1t9r). 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 5A, PDB code: 1t9r:

Zinc binding site 1 out of 1 in 1t9r

Go back to Zinc Binding Sites List in 1t9r
Zinc binding site 1 out of 1 in the Catalytic Domain of Human Phosphodiesterase 5A


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 5A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:49.0
occ:1.00
O3 A:PO4102 1.7 53.6 1.0
OD1 A:ASP764 2.0 38.7 1.0
NE2 A:HIS617 2.1 32.0 1.0
NE2 A:HIS653 2.1 36.8 1.0
P A:PO4102 2.8 57.2 1.0
CG A:ASP764 2.9 33.9 1.0
CD2 A:HIS617 2.9 31.0 1.0
O1 A:PO4102 3.0 56.8 1.0
CE1 A:HIS653 3.1 33.9 1.0
CD2 A:HIS653 3.1 34.3 1.0
CE1 A:HIS617 3.1 31.9 1.0
OD2 A:ASP764 3.2 34.0 1.0
OD2 A:ASP654 3.5 34.9 1.0
O2 A:PO4102 3.7 54.4 1.0
O4 A:PO4102 4.0 60.2 1.0
CG A:HIS617 4.1 30.8 1.0
CG A:ASP654 4.1 35.5 1.0
OD1 A:ASP654 4.2 32.7 1.0
ND1 A:HIS653 4.2 35.3 1.0
ND1 A:HIS617 4.2 28.1 1.0
CG A:HIS653 4.2 33.8 1.0
OG1 A:THR621 4.2 33.6 1.0
CB A:ASP764 4.3 32.6 1.0
CE1 A:HIS678 4.4 36.7 1.0
O A:ASP764 4.6 32.2 1.0
CA A:ASP764 4.6 31.8 1.0
ND1 A:HIS678 4.8 39.0 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: Wed Dec 16 03:04:21 2020

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