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Magnesium in PDB 1rs0: Crystal Structure Analysis of the Bb Segment of Factor B Complexed with Di-Isopropyl-Phosphate (Dip)

Enzymatic activity of Crystal Structure Analysis of the Bb Segment of Factor B Complexed with Di-Isopropyl-Phosphate (Dip)

All present enzymatic activity of Crystal Structure Analysis of the Bb Segment of Factor B Complexed with Di-Isopropyl-Phosphate (Dip):
3.4.21.47;

Protein crystallography data

The structure of Crystal Structure Analysis of the Bb Segment of Factor B Complexed with Di-Isopropyl-Phosphate (Dip), PDB code: 1rs0 was solved by K.Ponnuraj, Y.Xu, K.Macon, D.Moore, J.E.Volanakis, S.V.Narayana, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.82 / 2.60
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 98.449, 98.449, 125.678, 90.00, 90.00, 120.00
R / Rfree (%) 21.2 / 25.1

Other elements in 1rs0:

The structure of Crystal Structure Analysis of the Bb Segment of Factor B Complexed with Di-Isopropyl-Phosphate (Dip) also contains other interesting chemical elements:

Iodine (I) 2 atoms
Sodium (Na) 7 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure Analysis of the Bb Segment of Factor B Complexed with Di-Isopropyl-Phosphate (Dip) (pdb code 1rs0). 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 Analysis of the Bb Segment of Factor B Complexed with Di-Isopropyl-Phosphate (Dip), PDB code: 1rs0:

Magnesium binding site 1 out of 1 in 1rs0

Go back to Magnesium Binding Sites List in 1rs0
Magnesium binding site 1 out of 1 in the Crystal Structure Analysis of the Bb Segment of Factor B Complexed with Di-Isopropyl-Phosphate (Dip)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure Analysis of the Bb Segment of Factor B Complexed with Di-Isopropyl-Phosphate (Dip) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg749

b:51.5
occ:1.00
 OG A:SER255 2.1 38.7 1.0
OG A:SER253 2.3 41.6 1.0
O A:HOH946 2.4 17.2 1.0
OG1 A:THR328 2.4 34.9 1.0
O A:HOH945 2.6 27.0 1.0
CB A:SER255 3.4 35.0 1.0
O A:HOH947 3.4 26.1 1.0
CB A:SER253 3.4 37.4 1.0
CB A:THR328 3.5 33.4 1.0
CG2 A:THR328 3.8 33.0 1.0
O A:LEU366 3.8 40.7 1.0
N A:SER255 4.1 34.7 1.0
OD1 A:ASP364 4.2 35.6 1.0
ND2 A:ASN368 4.3 46.4 1.0
CA A:SER255 4.3 35.0 1.0
OD1 A:ASP251 4.4 27.7 1.0
OD2 A:ASP364 4.4 30.4 1.0
OD2 A:ASP251 4.6 27.9 1.0
CA A:SER253 4.7 35.9 1.0
CG A:ASP364 4.7 32.0 1.0
CA A:THR328 4.8 33.2 1.0
C A:LEU366 4.8 38.4 1.0
N A:ASP254 4.8 37.6 1.0
C A:SER253 4.8 36.2 1.0
CB A:LEU366 4.9 38.1 1.0
CG A:ASP251 4.9 29.9 1.0

Reference:

K.Ponnuraj, Y.Xu, K.Macon, D.Moore, J.E.Volanakis, S.V.Narayana. Structural Analysis of Engineered Bb Fragment of Complement Factor B: Insights Into the Activation Mechanism of the Alternative Pathway C3-Convertase. Mol.Cell V. 14 17 2004.
ISSN: ISSN 1097-2765
PubMed: 15068800
DOI: 10.1016/S1097-2765(04)00160-1
Page generated: Tue Aug 13 13:06:32 2024

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