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Zinc in PDB 1zeb: X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp

Enzymatic activity of X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp

All present enzymatic activity of X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp:
3.1.3.1;

Protein crystallography data

The structure of X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp, PDB code: 1zeb was solved by P.Llinas, E.A.Stura, A.Menez, Z.Kiss, T.Stigbrand, J.L.Millan, M.H.Le Du, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.96 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 89.022, 113.894, 106.594, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 19.7

Other elements in 1zeb:

The structure of X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp (pdb code 1zeb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp, PDB code: 1zeb:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1zeb

Go back to Zinc Binding Sites List in 1zeb
Zinc binding site 1 out of 2 in the X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:14.9
occ:1.00
OD1 A:ASP316 2.0 10.2 1.0
NE2 A:HIS432 2.1 12.8 1.0
O3P A:SEP92 2.1 14.5 1.0
OD2 A:ASP316 2.1 12.4 1.0
NE2 A:HIS320 2.1 14.6 1.0
CG A:ASP316 2.4 11.8 1.0
CD2 A:HIS432 3.0 13.0 1.0
CE1 A:HIS432 3.0 12.3 1.0
CE1 A:HIS320 3.1 14.8 1.0
CD2 A:HIS320 3.1 14.9 1.0
P A:SEP92 3.2 15.3 1.0
O1P A:SEP92 3.5 15.6 1.0
O A:HOH965 3.8 14.2 1.0
O2P A:SEP92 3.8 12.8 1.0
ZN A:ZN902 4.0 14.9 1.0
CB A:ASP316 4.0 12.9 1.0
CE1 A:HIS358 4.1 13.0 1.0
NE2 A:HIS358 4.2 12.2 1.0
ND1 A:HIS432 4.2 12.9 1.0
ND1 A:HIS320 4.2 15.4 1.0
CG A:HIS432 4.2 12.9 1.0
CG A:HIS320 4.2 14.4 1.0
CE1 A:HIS360 4.4 14.9 1.0
OD1 A:ASP42 4.5 14.2 1.0
OG A:SEP92 4.5 15.3 1.0
NE2 A:HIS360 4.5 11.9 1.0
CA A:ASP316 4.9 13.2 1.0
O A:ASP316 5.0 14.4 1.0

Zinc binding site 2 out of 2 in 1zeb

Go back to Zinc Binding Sites List in 1zeb
Zinc binding site 2 out of 2 in the X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn902

b:14.9
occ:1.00
OD1 A:ASP42 2.0 14.2 1.0
OD2 A:ASP357 2.0 12.7 1.0
NE2 A:HIS358 2.1 12.2 1.0
O3P A:SEP92 2.1 14.5 1.0
OG A:SEP92 2.2 15.3 1.0
P A:SEP92 2.7 15.3 1.0
CG A:ASP42 2.8 12.0 1.0
OD2 A:ASP42 2.8 10.9 1.0
CG A:ASP357 2.9 13.4 1.0
CD2 A:HIS358 3.0 12.2 1.0
CE1 A:HIS358 3.0 13.0 1.0
OD1 A:ASP357 3.1 10.8 1.0
CB A:SEP92 3.4 14.1 1.0
OD2 A:ASP316 3.6 12.4 1.0
O1P A:SEP92 3.8 15.6 1.0
O2P A:SEP92 3.8 12.8 1.0
CG A:ASP316 3.9 11.8 1.0
CA A:SEP92 3.9 14.3 1.0
ZN A:ZN901 4.0 14.9 1.0
CE1 A:HIS432 4.1 12.3 1.0
CG A:HIS358 4.1 11.0 1.0
ND1 A:HIS358 4.1 11.2 1.0
NE2 A:HIS432 4.1 12.8 1.0
CB A:ASP42 4.2 12.7 1.0
OD1 A:ASP316 4.2 10.2 1.0
N A:SEP92 4.2 14.2 1.0
CB A:ASP357 4.3 12.6 1.0
N A:GLY43 4.3 12.9 1.0
O A:HOH942 4.5 13.7 1.0
CA A:ASP42 4.5 12.6 1.0
CB A:ASP316 4.5 12.9 1.0
C A:ASP42 4.6 12.6 1.0
O A:HOH965 4.6 14.2 1.0
O A:HOH927 4.7 12.5 1.0
MG A:MG903 4.7 10.8 1.0
ND1 A:HIS432 4.8 12.9 1.0
C A:ASP91 4.9 14.3 1.0
CD2 A:HIS432 5.0 13.0 1.0
CA A:GLY43 5.0 12.6 1.0

Reference:

P.Llinas, E.A.Stura, A.Menez, Z.Kiss, T.Stigbrand, J.L.Millan, M.H.Le Du. Structural Studies of Human Placental Alkaline Phosphatase in Complex with Functional Ligands. J.Mol.Biol. V. 350 441 2005.
ISSN: ISSN 0022-2836
PubMed: 15946677
DOI: 10.1016/J.JMB.2005.04.068
Page generated: Wed Oct 16 21:12:58 2024

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