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Magnesium in PDB 3tp4: Crystal Structure of Engineered Protein at the Resolution 1.98A, Northeast Structural Genomics Consortium Target OR128

Protein crystallography data

The structure of Crystal Structure of Engineered Protein at the Resolution 1.98A, Northeast Structural Genomics Consortium Target OR128, PDB code: 3tp4 was solved by A.Kuzin, M.Su, J.Seetharaman, S.Rajagopalan, J.K.Everett, R.Nair, T.B.Acton, B.Rost, D.Baker, G.T.Montelione, J.F.Hunt, L.Tong, Northeaststructural Genomics Consortium (Nesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.26 / 1.98
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 88.666, 113.943, 116.815, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 21.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Engineered Protein at the Resolution 1.98A, Northeast Structural Genomics Consortium Target OR128 (pdb code 3tp4). 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 Engineered Protein at the Resolution 1.98A, Northeast Structural Genomics Consortium Target OR128, PDB code: 3tp4:

Magnesium binding site 1 out of 1 in 3tp4

Go back to Magnesium Binding Sites List in 3tp4
Magnesium binding site 1 out of 1 in the Crystal Structure of Engineered Protein at the Resolution 1.98A, Northeast Structural Genomics Consortium Target OR128


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 Engineered Protein at the Resolution 1.98A, Northeast Structural Genomics Consortium Target OR128 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg476

b:35.1
occ:1.00
O B:ASP349 2.3 30.6 1.0
O B:ALA347 2.4 32.5 1.0
O B:THR352 2.4 30.9 1.0
OG1 B:THR352 2.4 26.6 1.0
O B:HOH810 2.5 41.0 1.0
C B:THR352 3.2 32.5 1.0
C B:ALA347 3.4 33.1 1.0
C B:ASP349 3.4 29.7 1.0
CB B:THR352 3.5 28.1 1.0
CA B:THR352 3.6 33.2 1.0
N B:THR352 3.7 28.1 1.0
N B:ASP349 3.8 31.8 1.0
C B:ALA348 3.8 33.6 1.0
CE1 B:PHE354 4.0 28.3 1.0
CD1 B:PHE354 4.0 27.3 1.0
O B:ALA348 4.1 34.3 1.0
CA B:ASP349 4.2 34.0 1.0
O B:TYR346 4.2 27.5 1.0
N B:ALA348 4.2 27.4 1.0
CA B:ALA347 4.3 29.7 1.0
CA B:ALA348 4.3 34.4 1.0
N B:LEU353 4.4 25.8 1.0
N B:PRO350 4.4 36.7 1.0
C B:PRO350 4.5 31.7 1.0
CA B:PRO350 4.5 37.4 1.0
OE1 B:GLU357 4.6 43.0 1.0
CB B:ASP349 4.7 28.8 1.0
OE2 B:GLU357 4.7 55.3 1.0
O B:PRO350 4.7 30.0 1.0
CG2 B:THR352 4.7 26.2 1.0
N B:PHE351 4.8 31.0 1.0
C B:PHE351 4.8 27.5 1.0
CA B:LEU353 4.9 28.9 1.0

Reference:

S.Rajagopalan, C.Wang, K.Yu, A.P.Kuzin, F.Richter, S.Lew, A.E.Miklos, M.L.Matthews, J.Seetharaman, M.Su, J.F.Hunt, B.F.Cravatt, D.Baker. Design of Activated Serine-Containing Catalytic Triads with Atomic-Level Accuracy. Nat.Chem.Biol. V. 10 386 2014.
ISSN: ISSN 1552-4450
PubMed: 24705591
DOI: 10.1038/NCHEMBIO.1498
Page generated: Thu Aug 15 12:10:53 2024

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