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Magnesium in PDB 4ks9: Crystal Structure of Malonyl-Coa Decarboxylase (RMET_2797) From Cupriavidus Metallidurans, Northeast Structural Genomics Consortium Target CRR76

Enzymatic activity of Crystal Structure of Malonyl-Coa Decarboxylase (RMET_2797) From Cupriavidus Metallidurans, Northeast Structural Genomics Consortium Target CRR76

All present enzymatic activity of Crystal Structure of Malonyl-Coa Decarboxylase (RMET_2797) From Cupriavidus Metallidurans, Northeast Structural Genomics Consortium Target CRR76:
4.1.1.9;

Protein crystallography data

The structure of Crystal Structure of Malonyl-Coa Decarboxylase (RMET_2797) From Cupriavidus Metallidurans, Northeast Structural Genomics Consortium Target CRR76, PDB code: 4ks9 was solved by F.Forouhar, T.H.Tran, S.Lew, J.Seetharaman, R.Xiao, T.B.Acton, J.K.Everett, G.T.Montelione, J.F.Hunt, L.Tong, Northeast Structural Genomicsconsortium (Nesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.75 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 191.015, 69.392, 74.362, 90.00, 103.80, 90.00
R / Rfree (%) 23.9 / 28.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Malonyl-Coa Decarboxylase (RMET_2797) From Cupriavidus Metallidurans, Northeast Structural Genomics Consortium Target CRR76 (pdb code 4ks9). 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 Malonyl-Coa Decarboxylase (RMET_2797) From Cupriavidus Metallidurans, Northeast Structural Genomics Consortium Target CRR76, PDB code: 4ks9:

Magnesium binding site 1 out of 1 in 4ks9

Go back to Magnesium Binding Sites List in 4ks9
Magnesium binding site 1 out of 1 in the Crystal Structure of Malonyl-Coa Decarboxylase (RMET_2797) From Cupriavidus Metallidurans, Northeast Structural Genomics Consortium Target CRR76


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 Malonyl-Coa Decarboxylase (RMET_2797) From Cupriavidus Metallidurans, Northeast Structural Genomics Consortium Target CRR76 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg501

b:29.6
occ:1.00
 O B:HOH701 2.2 26.4 1.0
O B:HOH611 2.2 22.2 1.0
O B:HOH601 2.3 17.8 1.0
O B:HOH646 2.5 27.7 1.0
OD2 B:ASP346 3.6 37.9 1.0
O B:HOH602 3.7 23.6 1.0
O B:PRO365 4.0 25.1 1.0
OD1 B:ASP346 4.0 35.5 1.0
O B:ALA366 4.2 35.4 1.0
CG1 B:VAL364 4.2 28.7 1.0
CA B:GLY342 4.2 36.8 1.0
CG B:ASP346 4.2 35.8 1.0
O B:HOH722 4.4 34.2 1.0
C B:GLY342 4.5 37.8 1.0
O B:GLY342 4.6 38.3 1.0
CB B:VAL364 4.6 29.5 1.0
C B:ALA366 4.8 33.6 1.0
CA B:ALA366 4.8 32.2 1.0
O B:VAL364 5.0 29.5 1.0
C B:PRO365 5.0 27.5 1.0

Reference:

D.S.Froese, F.Forouhar, T.H.Tran, M.Vollmar, Y.S.Kim, S.Lew, H.Neely, J.Seetharaman, Y.Shen, R.Xiao, T.B.Acton, J.K.Everett, G.Cannone, S.Puranik, P.Savitsky, T.Krojer, E.S.Pilka, W.Kiyani, W.H.Lee, B.D.Marsden, F.Von Delft, C.K.Allerston, L.Spagnolo, O.Gileadi, G.T.Montelione, U.Oppermann, W.W.Yue, L.Tong. Crystal Structures of Malonyl-Coenzyme A Decarboxylase Provide Insights Into Its Catalytic Mechanism and Disease-Causing Mutations. Structure V. 21 1182 2013.
ISSN: ISSN 0969-2126
PubMed: 23791943
DOI: 10.1016/J.STR.2013.05.001
Page generated: Sat Aug 17 03:56:42 2024

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