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Manganese in PDB 2qjc: Crystal Structure of A Putative Diadenosine Tetraphosphatase

Enzymatic activity of Crystal Structure of A Putative Diadenosine Tetraphosphatase

All present enzymatic activity of Crystal Structure of A Putative Diadenosine Tetraphosphatase:
3.6.1.41;

Protein crystallography data

The structure of Crystal Structure of A Putative Diadenosine Tetraphosphatase, PDB code: 2qjc was solved by R.Sugadev, S.K.Burley, S.Swaminathan, New York Sgx Researchcenter For Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.40 / 2.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.662, 62.207, 81.296, 90.00, 90.00, 90.00
R / Rfree (%) 24.7 / 28.1

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of A Putative Diadenosine Tetraphosphatase (pdb code 2qjc). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of A Putative Diadenosine Tetraphosphatase, PDB code: 2qjc:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2qjc

Go back to Manganese Binding Sites List in 2qjc
Manganese binding site 1 out of 2 in the Crystal Structure of A Putative Diadenosine Tetraphosphatase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of A Putative Diadenosine Tetraphosphatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn400

b:31.9
occ:1.00
OD2 A:ASP55 2.1 16.5 1.0
OD2 A:ASP26 2.2 25.4 1.0
O A:HOH535 2.2 23.5 1.0
O4 A:PO4500 2.3 47.4 1.0
NE2 A:HIS28 2.5 29.6 1.0
CG A:ASP55 3.2 21.4 1.0
CD2 A:HIS28 3.3 27.8 1.0
CG A:ASP26 3.3 26.9 1.0
P A:PO4500 3.4 47.1 1.0
O1 A:PO4500 3.4 46.1 1.0
CE1 A:HIS28 3.5 28.7 1.0
MN A:MN401 3.6 45.4 1.0
CB A:ASP55 3.7 20.3 1.0
CB A:ASP26 3.8 22.5 1.0
OD2 A:ASP222 4.0 23.2 1.0
O A:HIS204 4.1 23.5 1.0
OD1 A:ASP55 4.3 20.6 1.0
CD2 A:HIS82 4.4 28.8 1.0
O A:HOH510 4.4 29.5 1.0
OD1 A:ASP26 4.4 25.6 1.0
CA A:HIS204 4.4 21.1 1.0
O2 A:PO4500 4.5 46.0 1.0
CG A:HIS28 4.5 30.5 1.0
O3 A:PO4500 4.5 47.5 1.0
ND1 A:HIS28 4.5 29.6 1.0
CE1 A:HIS141 4.5 20.8 1.0
C A:HIS204 4.7 23.6 1.0
NE2 A:HIS141 4.8 21.9 1.0
NE2 A:HIS82 4.8 33.0 1.0
N A:HIS204 4.9 19.9 1.0

Manganese binding site 2 out of 2 in 2qjc

Go back to Manganese Binding Sites List in 2qjc
Manganese binding site 2 out of 2 in the Crystal Structure of A Putative Diadenosine Tetraphosphatase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of A Putative Diadenosine Tetraphosphatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:45.4
occ:1.00
ND2 A:ASN81 2.1 30.1 1.0
ND1 A:HIS204 2.3 27.1 1.0
NE2 A:HIS141 2.3 21.9 1.0
O4 A:PO4500 2.5 47.4 1.0
OD2 A:ASP55 2.8 16.5 1.0
CE1 A:HIS204 3.2 22.4 1.0
O A:HOH515 3.2 36.9 1.0
CE1 A:HIS141 3.2 20.8 1.0
CG A:ASN81 3.2 29.7 1.0
CG A:HIS204 3.4 25.6 1.0
CD2 A:HIS141 3.4 21.6 1.0
CG A:ASP55 3.5 21.4 1.0
MN A:MN400 3.6 31.9 1.0
OD1 A:ASP55 3.6 20.6 1.0
OD1 A:ASN81 3.7 32.6 1.0
CB A:HIS204 3.7 22.9 1.0
CA A:HIS204 3.8 21.1 1.0
P A:PO4500 3.8 47.1 1.0
O2 A:PO4500 3.9 46.0 1.0
O A:HIS204 4.1 23.5 1.0
CD2 A:HIS82 4.2 28.8 1.0
OD2 A:ASP26 4.2 25.4 1.0
NE2 A:HIS204 4.3 27.1 1.0
N A:ASN81 4.3 27.8 1.0
C A:HIS204 4.4 23.6 1.0
ND1 A:HIS141 4.4 21.5 1.0
O A:THR159 4.4 23.9 1.0
CD2 A:HIS204 4.4 25.6 1.0
CB A:ASN81 4.5 29.1 1.0
CG A:HIS141 4.5 22.1 1.0
O3 A:PO4500 4.6 47.5 1.0
CB A:ASP55 4.8 20.3 1.0
N A:HIS204 4.8 19.9 1.0
CA A:ASN81 4.9 27.4 1.0
NE2 A:HIS82 4.9 33.0 1.0
N A:HIS82 5.0 27.4 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: Sat Oct 5 15:05:31 2024

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