Magnesium in PDB 2win: C3 Convertase (C3BBB) Stabilized By Scin

All present enzymatic activity of C3 Convertase (C3BBB) Stabilized By Scin:
3.4.21.47;

The structure of C3 Convertase (C3BBB) Stabilized By Scin, PDB code: 2win was solved by J.Wu, B.J.Janssen, P.Gros, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.68 / 3.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	228.632, 121.491, 280.783, 90.00, 91.64, 90.00
R / Rfree (%)	25.3 / 26.8

The binding sites of Magnesium atom in the C3 Convertase (C3BBB) Stabilized By Scin (pdb code 2win). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the C3 Convertase (C3BBB) Stabilized By Scin, PDB code: 2win:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the C3 Convertase (C3BBB) Stabilized By Scin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of C3 Convertase (C3BBB) Stabilized By Scin within 5.0Å range: probe atom residue distance (Å) B Occ I:Mg1742 b:0.8 occ:1.00 OG1 I:THR328 2.1 0.0 1.0 OG I:SER255 2.1 0.3 1.0 OG I:SER253 2.1 0.6 1.0 OXT D:ASN1641 2.1 0.2 1.0 O I:HOH2001 2.7 0.1 1.0 O I:HOH2002 2.9 0.3 1.0 C D:ASN1641 3.0 0.0 1.0 CB I:SER253 3.2 0.8 1.0 O D:ASN1641 3.3 0.8 1.0 CB I:THR328 3.4 0.8 1.0 CB I:SER255 3.5 0.7 1.0 O I:SER326 3.8 0.3 1.0 CG2 I:THR328 3.9 0.6 1.0 O I:LEU366 3.9 0.8 1.0 N I:SER255 4.0 0.2 1.0 CG D:ASN1641 4.1 0.0 1.0 OD1 D:ASN1641 4.2 0.3 1.0 CA D:ASN1641 4.3 0.1 1.0 CB D:ASN1641 4.3 0.5 1.0 CA I:SER255 4.3 0.1 1.0 CA I:THR328 4.4 0.3 1.0 CA I:SER253 4.5 0.3 1.0 OD1 I:ASP251 4.5 0.9 1.0 ND2 I:ASN368 4.5 0.4 1.0 ND2 D:ASN1641 4.5 0.8 1.0 N I:THR328 4.6 0.1 1.0 C I:SER253 4.6 0.6 1.0 N I:ASP254 4.6 0.1 1.0 OD2 I:ASP364 4.7 0.5 1.0 OD1 I:ASP364 4.7 0.3 1.0 C I:GLY327 4.7 0.7 1.0 O I:GLY327 4.7 0.3 1.0 OD2 I:ASP251 5.0 0.2 1.0 C I:SER326 5.0 0.1 1.0

Magnesium binding site 2 out of 4 in the C3 Convertase (C3BBB) Stabilized By Scin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of C3 Convertase (C3BBB) Stabilized By Scin within 5.0Å range: probe atom residue distance (Å) B Occ J:Mg1742 b:0.6 occ:1.00 OG J:SER255 2.1 0.5 1.0 OG1 J:THR328 2.1 0.1 1.0 OG J:SER253 2.1 0.8 1.0 OXT H:ASN1641 2.1 0.8 1.0 O J:HOH2002 2.6 0.2 1.0 O J:HOH2001 2.8 0.3 1.0 C H:ASN1641 2.9 0.5 1.0 O H:ASN1641 3.1 0.2 1.0 CB J:SER253 3.2 0.8 1.0 OD1 H:ASN1641 3.4 0.2 1.0 CB J:THR328 3.4 0.0 1.0 CB J:SER255 3.5 0.7 1.0 O J:SER326 3.7 0.6 1.0 CG H:ASN1641 3.9 0.8 1.0 CG2 J:THR328 4.0 0.2 1.0 N J:SER255 4.0 0.5 1.0 O J:LEU366 4.0 0.8 1.0 CA H:ASN1641 4.1 0.8 1.0 CA J:SER255 4.3 0.6 1.0 CA J:SER253 4.4 0.2 1.0 ND2 H:ASN1641 4.5 0.2 1.0 CA J:THR328 4.5 0.4 1.0 CB H:ASN1641 4.5 0.5 1.0 OD1 J:ASP251 4.5 0.4 1.0 N J:ASP254 4.5 1.0 1.0 C J:SER253 4.5 0.9 1.0 ND2 J:ASN368 4.5 0.8 1.0 N J:THR328 4.6 0.2 1.0 C J:GLY327 4.7 0.6 1.0 O J:GLY327 4.7 0.2 1.0 OD1 J:ASP364 4.7 0.7 1.0 OD2 J:ASP364 4.8 0.3 1.0 C J:SER326 4.9 0.7 1.0 OD2 J:ASP251 5.0 0.9 1.0

Magnesium binding site 3 out of 4 in the C3 Convertase (C3BBB) Stabilized By Scin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of C3 Convertase (C3BBB) Stabilized By Scin within 5.0Å range: probe atom residue distance (Å) B Occ K:Mg1742 b:0.1 occ:1.00 OG1 K:THR328 2.1 0.8 1.0 OG K:SER255 2.1 0.7 1.0 OG K:SER253 2.1 0.7 1.0 OXT F:ASN1641 2.1 0.0 1.0 O F:ASN1641 2.6 0.3 1.0 C F:ASN1641 2.8 0.1 1.0 O K:HOH2001 2.8 0.5 1.0 O K:HOH2002 3.0 0.1 1.0 CB K:SER253 3.2 0.8 1.0 CB K:THR328 3.4 0.9 1.0 CB K:SER255 3.5 0.1 1.0 O K:SER326 3.7 0.8 1.0 O K:LEU366 3.9 0.0 1.0 CG2 K:THR328 3.9 0.0 1.0 N K:SER255 4.0 1.0 1.0 CA F:ASN1641 4.3 0.4 1.0 CA K:SER255 4.4 0.7 1.0 CA K:THR328 4.4 0.6 1.0 CA K:SER253 4.5 0.1 1.0 ND2 K:ASN368 4.5 0.7 1.0 OD1 K:ASP251 4.5 0.4 1.0 N K:THR328 4.5 0.5 1.0 N K:ASP254 4.6 0.7 1.0 C K:SER253 4.6 0.3 1.0 C K:GLY327 4.7 0.5 1.0 O K:GLY327 4.7 0.1 1.0 OD1 K:ASP364 4.7 0.0 1.0 OD2 K:ASP364 4.8 0.2 1.0 CB F:ASN1641 4.8 0.6 1.0 C K:SER326 4.9 0.0 1.0

Magnesium binding site 4 out of 4 in the C3 Convertase (C3BBB) Stabilized By Scin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of C3 Convertase (C3BBB) Stabilized By Scin within 5.0Å range: probe atom residue distance (Å) B Occ L:Mg1742 b:0.2 occ:1.00 OG1 L:THR328 2.1 0.5 1.0 OG L:SER255 2.1 0.2 1.0 OG L:SER253 2.1 1.0 1.0 OXT B:ASN1641 2.1 0.8 1.0 O L:HOH2001 2.6 0.6 1.0 C B:ASN1641 2.9 0.5 1.0 O B:HOH2001 2.9 0.3 1.0 O B:ASN1641 3.1 0.8 1.0 CB L:SER253 3.2 0.9 1.0 CB L:THR328 3.4 0.5 1.0 CB L:SER255 3.5 1.0 1.0 O L:SER326 3.8 0.9 1.0 O L:LEU366 3.9 0.6 1.0 CG2 L:THR328 3.9 0.2 1.0 N L:SER255 4.0 0.6 1.0 CA B:ASN1641 4.2 0.5 1.0 CG B:ASN1641 4.3 0.9 1.0 OD1 B:ASN1641 4.3 0.2 1.0 CA L:SER255 4.3 0.9 1.0 CB B:ASN1641 4.4 0.7 1.0 CA L:THR328 4.4 0.7 1.0 CA L:SER253 4.5 0.1 1.0 OD1 L:ASP251 4.5 0.3 1.0 ND2 L:ASN368 4.5 0.4 1.0 N L:THR328 4.6 0.9 1.0 C L:SER253 4.6 0.8 1.0 N L:ASP254 4.6 0.8 1.0 OD2 L:ASP364 4.7 0.4 1.0 OD1 L:ASP364 4.7 0.2 1.0 C L:GLY327 4.7 0.7 1.0 O L:GLY327 4.7 0.3 1.0 ND2 B:ASN1641 4.7 0.3 1.0 OD2 L:ASP251 5.0 0.3 1.0 C L:SER326 5.0 0.0 1.0

S.H.Rooijakkers, J.Wu, M.Ruyken, R.Van Domselaar, K.L.Planken, A.Tzekou, D.Ricklin, J.D.Lambris, B.J.Janssen, J.A.Van Strijp, P.Gros. Structural and Functional Implications of the Alternative Complement Pathway C3 Convertase Stabilized By A Staphylococcal Inhibitor. Nat. Immunol. V. 10 721 2009.
ISSN: ESSN 1529-2916
PubMed: 19503103
DOI: 10.1038/NI.1756