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Magnesium in PDB 2p27: Crystal Structure of Human Pyridoxal Phosphate Phosphatase with MG2+ at 1.9 A Resolution

Enzymatic activity of Crystal Structure of Human Pyridoxal Phosphate Phosphatase with MG2+ at 1.9 A Resolution

All present enzymatic activity of Crystal Structure of Human Pyridoxal Phosphate Phosphatase with MG2+ at 1.9 A Resolution:
3.1.3.74;

Protein crystallography data

The structure of Crystal Structure of Human Pyridoxal Phosphate Phosphatase with MG2+ at 1.9 A Resolution, PDB code: 2p27 was solved by U.A.Ramagopal, J.Freeman, M.Izuka, R.Toro, J.M.Sauder, S.K.Burley, S.C.Almo, New York Sgx Research Center For Structural Genomics(Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.34 / 1.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 54.245, 54.245, 213.182, 90.00, 90.00, 90.00
R / Rfree (%) 21.1 / 25

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Pyridoxal Phosphate Phosphatase with MG2+ at 1.9 A Resolution (pdb code 2p27). 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 Crystal Structure of Human Pyridoxal Phosphate Phosphatase with MG2+ at 1.9 A Resolution, PDB code: 2p27:

Magnesium binding site 1 out of 1 in 2p27

Go back to Magnesium Binding Sites List in 2p27
Magnesium binding site 1 out of 1 in the Crystal Structure of Human Pyridoxal Phosphate Phosphatase with MG2+ at 1.9 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human Pyridoxal Phosphate Phosphatase with MG2+ at 1.9 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg307

b:20.0
occ:1.00
 OD2 A:ASP27 2.0 20.3 1.0
OD1 A:ASP240 2.0 22.1 1.0
O A:HOH308 2.1 19.7 1.0
O A:ASP29 2.1 20.4 0.5
O A:HOH310 2.1 20.7 1.0
O A:ASP29 2.1 20.0 0.5
O A:HOH309 2.2 19.3 1.0
CG A:ASP27 2.9 22.0 1.0
CG A:ASP240 3.1 19.6 1.0
C A:ASP29 3.3 21.1 0.5
C A:ASP29 3.3 20.8 0.5
OD1 A:ASP27 3.3 21.0 1.0
OD2 A:ASP240 3.4 19.3 1.0
OD2 A:ASP245 4.0 22.2 1.0
O A:HOH343 4.0 27.1 1.0
CA A:ASP29 4.1 21.1 0.5
CA A:ASP29 4.1 21.6 0.5
N A:ASP29 4.1 21.4 0.5
N A:ASP29 4.1 21.1 0.5
CB A:ASP29 4.2 21.6 0.5
CB A:ASP27 4.2 20.4 1.0
N A:GLY30 4.3 20.7 1.0
O A:HOH377 4.3 28.5 1.0
CB A:ASP29 4.4 22.4 0.5
CB A:ASP240 4.4 20.8 1.0
CA A:GLY30 4.5 20.3 1.0
CG2 A:VAL31 4.5 20.6 1.0
O A:HOH391 4.5 34.5 1.0
N A:ASP240 4.6 20.8 1.0
C A:CYS28 4.8 21.1 1.0
O A:HOH313 4.8 27.0 1.0
O A:HOH317 4.9 22.5 1.0
CG A:ASP245 4.9 25.0 1.0
C A:GLY30 4.9 20.4 1.0
N A:CYS28 4.9 20.1 1.0
OD1 A:ASP245 5.0 22.9 1.0
CA A:ASP240 5.0 21.3 1.0

Reference:

S.C.Almo, J.B.Bonanno, J.M.Sauder, S.Emtage, T.P.Dilorenzo, V.Malashkevich, S.R.Wasserman, S.Swaminathan, S.Eswaramoorthy, R.Agarwal, D.Kumaran, M.Madegowda, S.Ragumani, Y.Patskovsky, J.Alvarado, U.A.Ramagopal, J.Faber-Barata, M.R.Chance, A.Sali, A.Fiser, Z.Y.Zhang, D.S.Lawrence, S.K.Burley. Structural Genomics of Protein Phosphatases. J.Struct.Funct.Genom. V. 8 121 2007.
ISSN: ISSN 1345-711X
PubMed: 18058037
DOI: 10.1007/S10969-007-9036-1
Page generated: Wed Aug 14 02:02:38 2024

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