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Zinc in PDB 1t9s: Catalytic Domain of Human Phosphodiesterase 5A in Complex with Gmp

Enzymatic activity of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Gmp

All present enzymatic activity of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Gmp:
3.1.4.17;

Protein crystallography data

The structure of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Gmp, PDB code: 1t9s 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) 69.01 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 61.969, 90.872, 68.991, 90.00, 98.07, 90.00
R / Rfree (%) 17.5 / 21.2

Other elements in 1t9s:

The structure of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Gmp also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Catalytic Domain of Human Phosphodiesterase 5A in Complex with Gmp (pdb code 1t9s). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Catalytic Domain of Human Phosphodiesterase 5A in Complex with Gmp, PDB code: 1t9s:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1t9s

Go back to Zinc Binding Sites List in 1t9s
Zinc binding site 1 out of 2 in the Catalytic Domain of Human Phosphodiesterase 5A in Complex with Gmp


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 in Complex with Gmp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:13.6
occ:1.00
O2P A:5GP859 2.0 11.9 1.0
OD2 A:ASP654 2.0 9.2 1.0
O A:HOH1151 2.1 12.7 1.0
OD1 A:ASP764 2.1 7.4 1.0
NE2 A:HIS653 2.1 9.3 1.0
NE2 A:HIS617 2.1 6.7 1.0
CD2 A:HIS653 3.0 7.2 1.0
CG A:ASP764 3.1 8.3 1.0
CD2 A:HIS617 3.1 5.0 1.0
CG A:ASP654 3.1 7.6 1.0
CE1 A:HIS617 3.1 5.8 1.0
CE1 A:HIS653 3.2 8.3 1.0
P A:5GP859 3.3 16.3 1.0
OD2 A:ASP764 3.3 8.4 1.0
O1P A:5GP859 3.6 13.8 1.0
MG A:MG2 3.6 11.5 1.0
OD1 A:ASP654 3.6 8.7 1.0
O A:HOH1155 3.8 12.9 1.0
O5' A:5GP859 4.1 16.3 1.0
CG A:HIS653 4.2 7.7 1.0
ND1 A:HIS617 4.2 5.5 1.0
CG A:HIS617 4.3 5.5 1.0
ND1 A:HIS653 4.3 7.2 1.0
CB A:ASP654 4.3 6.3 1.0
O3P A:5GP859 4.4 15.4 1.0
CB A:ASP764 4.4 8.3 1.0
CD2 A:HIS613 4.6 9.0 1.0
C5' A:5GP859 4.7 17.9 1.0
O A:HOH1152 4.8 10.4 1.0
O A:ASP764 4.9 9.0 1.0
CA A:ASP764 4.9 8.3 1.0
OG1 A:THR621 5.0 6.7 1.0

Zinc binding site 2 out of 2 in 1t9s

Go back to Zinc Binding Sites List in 1t9s
Zinc binding site 2 out of 2 in the Catalytic Domain of Human Phosphodiesterase 5A in Complex with Gmp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Catalytic Domain of Human Phosphodiesterase 5A in Complex with Gmp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1

b:14.3
occ:1.00
O B:HOH1133 2.0 13.1 1.0
O2P B:5GP859 2.0 13.7 1.0
OD2 B:ASP654 2.0 8.7 1.0
OD1 B:ASP764 2.1 7.2 1.0
NE2 B:HIS653 2.1 9.1 1.0
NE2 B:HIS617 2.1 7.5 1.0
CD2 B:HIS653 3.0 8.7 1.0
CG B:ASP764 3.0 8.5 1.0
CE1 B:HIS617 3.1 7.3 1.0
CG B:ASP654 3.1 6.3 1.0
CE1 B:HIS653 3.1 8.4 1.0
CD2 B:HIS617 3.2 7.6 1.0
OD2 B:ASP764 3.3 8.8 1.0
P B:5GP859 3.3 18.4 1.0
OD1 B:ASP654 3.6 6.6 1.0
O1P B:5GP859 3.6 13.2 1.0
MG B:MG2 3.6 11.1 1.0
O B:HOH1137 3.9 13.5 1.0
O5' B:5GP859 4.0 17.2 1.0
CG B:HIS653 4.2 7.1 1.0
ND1 B:HIS617 4.2 8.1 1.0
ND1 B:HIS653 4.2 7.7 1.0
CG B:HIS617 4.3 6.9 1.0
CB B:ASP654 4.3 6.3 1.0
CB B:ASP764 4.4 7.8 1.0
O3P B:5GP859 4.5 16.1 1.0
CD2 B:HIS613 4.6 9.4 1.0
C5' B:5GP859 4.7 17.9 1.0
O B:HOH1134 4.8 10.6 1.0
O B:ASP764 4.9 7.8 1.0
CA B:ASP764 5.0 7.8 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 Oct 16 19:03:35 2024

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