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Magnesium in PDB 1ka1: The Papase HAL2P Complexed with Calcium and Magnesium Ions and Reaction Substrate: Pap

Enzymatic activity of The Papase HAL2P Complexed with Calcium and Magnesium Ions and Reaction Substrate: Pap

All present enzymatic activity of The Papase HAL2P Complexed with Calcium and Magnesium Ions and Reaction Substrate: Pap:
3.1.3.7;

Protein crystallography data

The structure of The Papase HAL2P Complexed with Calcium and Magnesium Ions and Reaction Substrate: Pap, PDB code: 1ka1 was solved by S.Patel, A.Albert, T.L.Blundell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.875, 44.968, 72.110, 90.00, 110.72, 90.00
R / Rfree (%) 13.3 / 16.9

Other elements in 1ka1:

The structure of The Papase HAL2P Complexed with Calcium and Magnesium Ions and Reaction Substrate: Pap also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Papase HAL2P Complexed with Calcium and Magnesium Ions and Reaction Substrate: Pap (pdb code 1ka1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the The Papase HAL2P Complexed with Calcium and Magnesium Ions and Reaction Substrate: Pap, PDB code: 1ka1:

Magnesium binding site 1 out of 1 in 1ka1

Go back to Magnesium Binding Sites List in 1ka1
Magnesium binding site 1 out of 1 in the The Papase HAL2P Complexed with Calcium and Magnesium Ions and Reaction Substrate: Pap


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Papase HAL2P Complexed with Calcium and Magnesium Ions and Reaction Substrate: Pap within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:11.7
occ:1.00
 O1P A:A3P601 2.0 16.6 1.0
OD1 A:ASP294 2.1 10.8 1.0
OD1 A:ASP145 2.2 19.0 1.0
O3' A:A3P601 2.3 24.0 1.0
OD2 A:ASP142 2.3 13.3 1.0
O A:HOH639 2.7 13.2 1.0
P1 A:A3P601 2.8 28.1 1.0
C3' A:A3P601 3.0 25.3 1.0
CG A:ASP294 3.2 9.0 1.0
O2' A:A3P601 3.3 38.7 1.0
CG A:ASP145 3.4 9.0 1.0
CG A:ASP142 3.6 10.0 1.0
OD2 A:ASP294 3.6 11.2 1.0
C4' A:A3P601 3.6 22.1 1.0
O3P A:A3P601 3.6 25.8 1.0
C2' A:A3P601 3.7 29.5 1.0
CA A:CA401 3.8 8.9 1.0
O2P A:A3P601 4.0 13.6 1.0
CA A:ASP145 4.0 8.1 1.0
CB A:ASP145 4.1 9.7 1.0
CD1 A:TRP293 4.2 9.2 1.0
OD1 A:ASP142 4.2 8.8 1.0
OD2 A:ASP145 4.3 15.9 1.0
C5' A:A3P601 4.3 20.6 1.0
OE1 A:GLU72 4.3 8.8 1.0
NE1 A:TRP293 4.3 9.0 1.0
CB A:ASP294 4.4 9.0 1.0
N A:GLY146 4.4 8.6 1.0
CB A:ASP142 4.6 7.4 1.0
CA A:ASP294 4.7 7.2 1.0
C A:ASP145 4.7 7.5 1.0
C1' A:A3P601 4.8 27.4 1.0
O A:HOH644 4.8 13.1 1.0
O A:ILE144 4.8 7.4 1.0
O4' A:A3P601 4.9 25.2 1.0
O A:HOH797 4.9 28.5 1.0
O A:HOH613 5.0 9.8 1.0

Reference:

S.Patel, M.Martinez-Ripoll, T.L.Blundell, A.Albert. Structural Enzymology of Li(+)-Sensitive/Mg(2+)-Dependent Phosphatases. J.Mol.Biol. V. 320 1087 2002.
ISSN: ISSN 0022-2836
PubMed: 12126627
DOI: 10.1016/S0022-2836(02)00564-8
Page generated: Sun Aug 10 00:06:38 2025

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