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Magnesium in PDB 2odp: Complement Component C2A, the Catalytic Fragment of C3- and C5- Convertase of Human Complement

Enzymatic activity of Complement Component C2A, the Catalytic Fragment of C3- and C5- Convertase of Human Complement

All present enzymatic activity of Complement Component C2A, the Catalytic Fragment of C3- and C5- Convertase of Human Complement:
3.4.21.43;

Protein crystallography data

The structure of Complement Component C2A, the Catalytic Fragment of C3- and C5- Convertase of Human Complement, PDB code: 2odp was solved by S.V.L.Narayana, V.Krishnan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.398, 83.819, 75.243, 90.00, 92.10, 90.00
R / Rfree (%) 20.7 / 25

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Complement Component C2A, the Catalytic Fragment of C3- and C5- Convertase of Human Complement (pdb code 2odp). 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 Complement Component C2A, the Catalytic Fragment of C3- and C5- Convertase of Human Complement, PDB code: 2odp:

Magnesium binding site 1 out of 1 in 2odp

Go back to Magnesium Binding Sites List in 2odp
Magnesium binding site 1 out of 1 in the Complement Component C2A, the Catalytic Fragment of C3- and C5- Convertase of Human Complement


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Complement Component C2A, the Catalytic Fragment of C3- and C5- Convertase of Human Complement within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg901

b:20.0
occ:1.00
O A:HOH902 1.9 21.5 1.0
O A:HOH903 2.0 24.0 1.0
OG A:SER242 2.0 22.2 1.0
OG1 A:THR317 2.1 19.1 1.0
OG A:SER244 2.2 24.0 1.0
O A:HOH904 2.2 20.1 1.0
CB A:SER242 3.0 23.7 1.0
CB A:SER244 3.3 29.2 1.0
CB A:THR317 3.3 19.1 1.0
O A:HOH978 3.3 22.3 1.0
CG2 A:THR317 3.6 19.6 1.0
N A:SER244 3.9 29.4 1.0
OD1 A:ASP240 4.0 17.0 1.0
OD2 A:ASP240 4.1 18.4 1.0
OD1 A:ASP356 4.1 23.7 1.0
CA A:SER244 4.2 28.4 1.0
O A:LYS358 4.2 21.9 1.0
OD2 A:ASP356 4.2 24.9 1.0
CA A:SER242 4.3 24.3 1.0
C A:SER242 4.4 26.4 1.0
CA A:THR317 4.4 19.5 1.0
CG A:ASP240 4.5 18.2 1.0
N A:GLN243 4.6 27.4 1.0
CG A:ASP356 4.6 25.3 1.0
N A:THR317 4.8 21.5 1.0
C A:SER244 4.8 28.9 1.0
N A:VAL245 4.9 29.1 1.0
C A:LYS358 4.9 22.7 1.0
O A:SER242 5.0 25.3 1.0
ND2 A:ASN360 5.0 24.5 1.0
CB A:LYS358 5.0 24.2 1.0

Reference:

V.Krishnan, Y.Xu, K.Macon, J.E.Volanakis, S.V.Narayana. The Crystal Structure of C2A, the Catalytic Fragment of Classical Pathway C3 and C5 Convertase of Human Complement. J.Mol.Biol. V. 367 224 2007.
ISSN: ISSN 0022-2836
PubMed: 17234210
DOI: 10.1016/J.JMB.2006.12.039
Page generated: Mon Dec 14 07:32:10 2020

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