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Magnesium in PDB 1six: Mycobacterium Tuberculosis Dutpase Complexed with Magnesium and Alpha, Beta-Imido-Dutp

Enzymatic activity of Mycobacterium Tuberculosis Dutpase Complexed with Magnesium and Alpha, Beta-Imido-Dutp

All present enzymatic activity of Mycobacterium Tuberculosis Dutpase Complexed with Magnesium and Alpha, Beta-Imido-Dutp:
3.6.1.23;

Protein crystallography data

The structure of Mycobacterium Tuberculosis Dutpase Complexed with Magnesium and Alpha, Beta-Imido-Dutp, PDB code: 1six was solved by M.R.Sawaya, S.Chan, B.Segelke, T.Lekin, H.Krupka, U.-S.Cho, M.Kim, M.So, C.-Y.Kim, C.M.Naranjo, Y.C.Rogers, M.S.Park, G.S.Waldo, I.Pashkov, D.Cascio, T.O.Yeates, J.L.Perry, T.C.Terwilliger, D.Eisenberg, Tb Structuralgenomics Consortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.30
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 54.822, 54.822, 84.210, 90.00, 90.00, 120.00
R / Rfree (%) 12 / 13.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mycobacterium Tuberculosis Dutpase Complexed with Magnesium and Alpha, Beta-Imido-Dutp (pdb code 1six). 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 Mycobacterium Tuberculosis Dutpase Complexed with Magnesium and Alpha, Beta-Imido-Dutp, PDB code: 1six:

Magnesium binding site 1 out of 1 in 1six

Go back to Magnesium Binding Sites List in 1six
Magnesium binding site 1 out of 1 in the Mycobacterium Tuberculosis Dutpase Complexed with Magnesium and Alpha, Beta-Imido-Dutp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mycobacterium Tuberculosis Dutpase Complexed with Magnesium and Alpha, Beta-Imido-Dutp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg171

b:14.3
occ:1.00
O1G A:DUP170 2.0 14.6 1.0
O1A A:DUP170 2.1 13.5 1.0
O A:HOH302 2.1 16.5 1.0
O A:HOH301 2.1 15.8 1.0
O1B A:DUP170 2.1 14.1 1.0
O A:HOH303 2.1 16.8 1.0
PB A:DUP170 3.2 14.2 1.0
PG A:DUP170 3.3 15.9 1.0
PA A:DUP170 3.3 13.1 1.0
O3B A:DUP170 3.5 16.1 1.0
N3A A:DUP170 3.6 14.1 1.0
O3G A:DUP170 4.0 19.8 1.0
OD1 A:ASP28 4.2 19.6 1.0
NE A:ARG64 4.2 15.5 1.0
O A:HOH322 4.2 19.3 1.0
O A:HOH349 4.2 21.0 1.0
O2A A:DUP170 4.3 14.0 1.0
NH2 A:ARG64 4.4 15.5 1.0
O5' A:DUP170 4.4 12.4 1.0
OD2 A:ASP28 4.4 23.9 1.0
O2G A:DUP170 4.4 18.8 1.0
C5' A:DUP170 4.5 13.2 1.0
O2B A:DUP170 4.5 15.2 1.0
OE1 A:GLN113 4.6 26.3 1.0
NE2 A:GLN113 4.7 24.2 1.0
CG A:ASP28 4.7 18.6 1.0
CB A:ALA20 4.8 24.2 1.0
CZ A:ARG64 4.8 14.2 1.0
O A:HOH354 4.9 23.9 1.0
CD A:GLN113 4.9 22.7 1.0

Reference:

S.Chan, B.Segelke, T.Lekin, H.Krupka, U.S.Cho, M.-Y.Kim, M.So, C.-Y.Kim, C.M.Naranjo, Y.C.Rogers, M.S.Park, G.S.Waldo, I.Pashkov, D.Cascio, J.L.Perry, M.R.Sawaya. Crystal Structure of the Mycobacterium Tuberculosis Dutpase: Insights Into the Catalytic Mechanism. J.Mol.Biol. V. 341 503 2004.
ISSN: ISSN 0022-2836
PubMed: 15276840
DOI: 10.1016/J.JMB.2004.06.028
Page generated: Tue Aug 13 13:44:22 2024

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