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Magnesium in PDB 3tyz: Crystal Structure of the Yersinia Pestis Dihydropteroate Synthetase with Substrate Transition State Complex.

Enzymatic activity of Crystal Structure of the Yersinia Pestis Dihydropteroate Synthetase with Substrate Transition State Complex.

All present enzymatic activity of Crystal Structure of the Yersinia Pestis Dihydropteroate Synthetase with Substrate Transition State Complex.:
2.5.1.15;

Protein crystallography data

The structure of Crystal Structure of the Yersinia Pestis Dihydropteroate Synthetase with Substrate Transition State Complex., PDB code: 3tyz was solved by Y.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.07
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 70.179, 50.522, 74.668, 90.00, 90.75, 90.00
R / Rfree (%) 19.4 / 22.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Yersinia Pestis Dihydropteroate Synthetase with Substrate Transition State Complex. (pdb code 3tyz). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Yersinia Pestis Dihydropteroate Synthetase with Substrate Transition State Complex., PDB code: 3tyz:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3tyz

Go back to Magnesium Binding Sites List in 3tyz
Magnesium binding site 1 out of 2 in the Crystal Structure of the Yersinia Pestis Dihydropteroate Synthetase with Substrate Transition State Complex.


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 the Yersinia Pestis Dihydropteroate Synthetase with Substrate Transition State Complex. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg281

b:23.9
occ:1.00
O2 A:POP279 2.1 29.0 1.0
OD1 A:ASN22 2.1 19.1 1.0
O A:HOH305 2.1 12.1 1.0
O A:HOH307 2.2 18.2 1.0
O5 A:POP279 2.2 26.0 1.0
O A:HOH306 2.2 17.4 1.0
CG A:ASN22 3.1 20.9 1.0
P1 A:POP279 3.3 29.9 1.0
P2 A:POP279 3.4 25.7 1.0
OG A:SER27 3.5 28.2 1.0
O1 A:POP279 3.7 30.3 1.0
O A:POP279 3.8 27.0 1.0
ND2 A:ASN22 3.8 20.0 1.0
NH2 A:ARG255 3.9 18.2 1.0
O4 A:POP279 3.9 25.6 1.0
O A:HOH318 4.3 21.0 1.0
CB A:ASN22 4.3 21.8 1.0
O A:GLU60 4.3 25.6 1.0
OD2 A:ASP96 4.4 22.0 1.0
O A:HOH311 4.4 13.3 1.0
C7 A:XHP278 4.4 24.5 1.0
O3 A:POP279 4.5 28.9 1.0
CB A:SER27 4.6 27.2 1.0
O6 A:POP279 4.6 25.4 1.0
O A:GLY58 4.6 23.1 1.0
CA A:GLY58 4.8 21.7 1.0
CA A:SER61 4.8 26.3 1.0
CA A:ASN22 4.8 21.8 1.0
C A:GLY58 4.9 22.9 1.0
C A:GLU60 5.0 26.1 1.0

Magnesium binding site 2 out of 2 in 3tyz

Go back to Magnesium Binding Sites List in 3tyz
Magnesium binding site 2 out of 2 in the Crystal Structure of the Yersinia Pestis Dihydropteroate Synthetase with Substrate Transition State Complex.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Yersinia Pestis Dihydropteroate Synthetase with Substrate Transition State Complex. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg281

b:37.5
occ:1.00
O2 B:POP279 2.0 31.6 1.0
O B:HOH284 2.0 17.8 1.0
O5 B:POP279 2.1 33.5 1.0
OD1 B:ASN22 2.1 32.4 1.0
O B:HOH283 2.1 14.7 1.0
O B:HOH282 2.4 21.3 1.0
P2 B:POP279 3.2 33.4 1.0
CG B:ASN22 3.2 32.6 1.0
P1 B:POP279 3.2 30.4 1.0
O4 B:POP279 3.5 33.8 1.0
O B:POP279 3.6 31.1 1.0
ND2 B:ASN22 3.8 31.1 1.0
OG B:SER27 3.8 35.3 1.0
NH2 B:ARG255 3.9 28.0 1.0
O1 B:POP279 4.0 29.9 1.0
C7 B:XHP278 4.2 31.5 1.0
OD2 B:ASP96 4.2 32.8 1.0
O B:HOH285 4.3 17.3 1.0
O B:HOH312 4.4 17.4 1.0
O3 B:POP279 4.4 30.5 1.0
O6 B:POP279 4.4 33.2 1.0
CB B:ASN22 4.4 33.9 1.0
O B:GLU60 4.6 36.1 1.0
O B:HOH323 4.6 20.4 1.0
CA B:SER61 4.7 35.4 1.0
CB B:SER27 4.8 34.2 1.0
O B:GLY58 4.8 37.2 1.0
CA B:GLY58 4.9 35.9 1.0
CA B:ASN22 4.9 34.5 1.0

Reference:

M.K.Yun, Y.Wu, Z.Li, Y.Zhao, M.B.Waddell, A.M.Ferreira, R.E.Lee, D.Bashford, S.W.White. Catalysis and Sulfa Drug Resistance in Dihydropteroate Synthase. Science V. 335 1110 2012.
ISSN: ISSN 0036-8075
PubMed: 22383850
DOI: 10.1126/SCIENCE.1214641
Page generated: Thu Aug 15 12:17:19 2024

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