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Manganese in PDB 2i6q: Complement Component C2A

Enzymatic activity of Complement Component C2A

All present enzymatic activity of Complement Component C2A:
3.4.21.43;

Protein crystallography data

The structure of Complement Component C2A, PDB code: 2i6q was solved by F.J.Milder, H.C.A.Raaijmakers, D.A.A.Vandeputte, A.Schouten, E.G.Huizinga, R.A.Romijn, W.Hemrika, A.Roos, M.R.Daha, P.Gros, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.50 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.482, 77.185, 70.858, 90.00, 109.55, 90.00
R / Rfree (%) 18.9 / 24

Manganese Binding Sites:

The binding sites of Manganese atom in the Complement Component C2A (pdb code 2i6q). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Complement Component C2A, PDB code: 2i6q:

Manganese binding site 1 out of 1 in 2i6q

Go back to Manganese Binding Sites List in 2i6q
Manganese binding site 1 out of 1 in the Complement Component C2A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Complement Component C2A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1001

b:10.8
occ:1.00
O A:HOH1003 2.0 10.3 1.0
O A:HOH1002 2.1 6.4 1.0
OG A:SER242 2.2 15.0 1.0
O8 A:MLI1004 2.2 11.2 1.0
OG1 A:THR317 2.2 14.0 1.0
OG A:SER244 2.2 12.3 1.0
C3 A:MLI1004 3.1 13.0 1.0
CB A:SER244 3.2 12.6 1.0
CB A:SER242 3.3 16.5 1.0
O9 A:MLI1004 3.3 11.8 1.0
CB A:THR317 3.4 15.3 1.0
CG2 A:THR317 3.8 13.1 1.0
N A:SER244 4.0 13.7 1.0
O A:LYS358 4.1 17.0 1.0
OD2 A:ASP356 4.1 10.7 1.0
O A:HOH56 4.1 27.7 1.0
CA A:SER244 4.1 13.1 1.0
OD1 A:ASP356 4.2 15.6 1.0
OD2 A:ASP240 4.2 17.3 1.0
OD1 A:ASP240 4.3 16.9 1.0
C1 A:MLI1004 4.4 13.8 1.0
CA A:SER242 4.5 15.9 1.0
C A:SER242 4.5 16.0 1.0
CA A:THR317 4.6 15.3 1.0
CG A:ASP356 4.6 13.1 1.0
N A:GLN243 4.7 14.7 1.0
CG A:ASP240 4.7 17.6 1.0
N A:VAL245 4.7 13.1 1.0
CB A:LYS358 4.7 16.8 1.0
ND2 A:ASN360 4.8 6.7 1.0
C A:SER244 4.8 13.0 1.0
N A:THR317 4.8 16.8 1.0
C A:LYS358 4.9 17.1 1.0
O A:SER242 4.9 16.2 1.0

Reference:

F.J.Milder, H.C.Raaijmakers, M.D.Vandeputte, A.Schouten, E.G.Huizinga, R.A.Romijn, W.Hemrika, A.Roos, M.R.Daha, P.Gros. Structure of Complement Component C2A: Implications For Convertase Formation and Substrate Binding. Structure V. 14 1587 2006.
ISSN: ISSN 0969-2126
PubMed: 17027507
DOI: 10.1016/J.STR.2006.08.008
Page generated: Sat Oct 5 14:26:17 2024

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