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Zinc in PDB 3mk2: Placental Alkaline Phosphatase Complexed with Phe

Enzymatic activity of Placental Alkaline Phosphatase Complexed with Phe

All present enzymatic activity of Placental Alkaline Phosphatase Complexed with Phe:
3.1.3.1;

Protein crystallography data

The structure of Placental Alkaline Phosphatase Complexed with Phe, PDB code: 3mk2 was solved by B.Stec, A.Cheltsov, J.L.Millan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 69.84 / 1.89
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 87.791, 114.944, 106.341, 90.00, 90.00, 90.00
R / Rfree (%) 12.3 / 16.3

Other elements in 3mk2:

The structure of Placental Alkaline Phosphatase Complexed with Phe 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 Placental Alkaline Phosphatase Complexed with Phe (pdb code 3mk2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Placental Alkaline Phosphatase Complexed with Phe, PDB code: 3mk2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3mk2

Go back to Zinc Binding Sites List in 3mk2
Zinc binding site 1 out of 2 in the Placental Alkaline Phosphatase Complexed with Phe


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Placental Alkaline Phosphatase Complexed with Phe within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:13.8
occ:1.00
NE2 A:HIS432 2.0 12.0 1.0
OD1 A:ASP316 2.0 12.3 1.0
NE2 A:HIS320 2.1 12.7 1.0
O3P A:SEP92 2.1 12.2 1.0
N A:PHE912 2.2 43.1 0.8
OD2 A:ASP316 2.4 11.4 1.0
CG A:ASP316 2.5 12.3 1.0
CD2 A:HIS432 3.0 12.0 1.0
CA A:PHE912 3.0 44.4 0.8
CE1 A:HIS432 3.0 13.8 1.0
CD2 A:HIS320 3.0 12.1 1.0
CE1 A:HIS320 3.1 13.2 1.0
P A:SEP92 3.2 13.4 1.0
O1P A:SEP92 3.6 14.0 1.0
O2P A:SEP92 3.9 13.6 1.0
O A:HOH1001 3.9 12.4 1.0
CD1 A:PHE912 4.0 44.9 0.8
C A:PHE912 4.0 44.4 0.8
CB A:ASP316 4.0 10.9 1.0
ZN A:ZN902 4.0 13.8 1.0
ND1 A:HIS432 4.1 11.1 1.0
CG A:HIS432 4.1 13.1 1.0
CB A:PHE912 4.2 44.4 0.8
CE1 A:HIS358 4.2 11.9 1.0
ND1 A:HIS320 4.2 12.7 1.0
CG A:HIS320 4.2 12.0 1.0
NE2 A:HIS358 4.3 12.0 1.0
CE1 A:HIS360 4.3 10.9 1.0
O A:PHE912 4.4 44.5 0.8
OD1 A:ASP42 4.5 11.3 1.0
CG A:PHE912 4.5 44.7 0.8
OG A:SEP92 4.6 13.6 1.0
NE2 A:HIS360 4.6 11.0 1.0
OXT A:PHE912 4.8 44.5 0.8
O A:ASP316 4.9 10.9 1.0
CA A:ASP316 4.9 11.0 1.0
C A:ASP316 5.0 10.8 1.0

Zinc binding site 2 out of 2 in 3mk2

Go back to Zinc Binding Sites List in 3mk2
Zinc binding site 2 out of 2 in the Placental Alkaline Phosphatase Complexed with Phe


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Placental Alkaline Phosphatase Complexed with Phe within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn902

b:13.8
occ:1.00
OD1 A:ASP42 1.8 11.3 1.0
OG A:SEP92 2.1 13.6 1.0
NE2 A:HIS358 2.1 12.0 1.0
OD2 A:ASP357 2.1 11.7 1.0
O3P A:SEP92 2.2 12.2 1.0
CG A:ASP42 2.7 10.6 1.0
P A:SEP92 2.9 13.4 1.0
CG A:ASP357 2.9 10.5 1.0
OD2 A:ASP42 2.9 11.9 1.0
CD2 A:HIS358 3.0 11.5 1.0
CE1 A:HIS358 3.1 11.9 1.0
OD1 A:ASP357 3.1 9.7 1.0
CB A:SEP92 3.4 11.8 1.0
OD2 A:ASP316 3.7 11.4 1.0
CA A:SEP92 3.9 12.6 1.0
O1P A:SEP92 3.9 14.0 1.0
CG A:ASP316 3.9 12.3 1.0
O2P A:SEP92 4.0 13.6 1.0
ZN A:ZN901 4.0 13.8 1.0
CE1 A:HIS432 4.1 13.8 1.0
CB A:ASP42 4.1 11.3 1.0
NE2 A:HIS432 4.1 12.0 1.0
ND1 A:HIS358 4.1 11.3 1.0
CG A:HIS358 4.1 11.2 1.0
N A:SEP92 4.2 13.0 1.0
N A:GLY43 4.2 10.7 1.0
OD1 A:ASP316 4.2 12.3 1.0
CB A:ASP357 4.3 10.2 1.0
O A:HOH1041 4.4 11.7 1.0
CA A:ASP42 4.4 10.8 1.0
C A:ASP42 4.5 10.3 1.0
CB A:ASP316 4.5 10.9 1.0
O A:HOH1001 4.7 12.4 1.0
MG A:MG903 4.7 10.8 1.0
O A:HOH1053 4.7 12.6 1.0
ND1 A:HIS432 4.9 11.1 1.0
C A:ASP91 4.9 12.8 1.0
CA A:GLY43 4.9 10.6 1.0
CD2 A:HIS432 4.9 12.0 1.0

Reference:

B.Stec, A.Cheltsov, J.L.Millan. Refined Structures of Placental Alkaline Phosphatase Show A Consistent Pattern of Interactions at the Peripheral Site. Acta Crystallogr.,Sect.F V. 66 866 2010.
ISSN: ESSN 1744-3091
PubMed: 20693656
DOI: 10.1107/S1744309110019767
Page generated: Sat Oct 26 09:34:16 2024

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