Calcium in PDB 5cis: The CUB1-Egf-CUB2 Domains of Rat Mbl-Associated Serine Protease-2 (Masp-2) Bound to CA2+

The structure of The CUB1-Egf-CUB2 Domains of Rat Mbl-Associated Serine Protease-2 (Masp-2) Bound to CA2+, PDB code: 5cis was solved by R.Nan, C.M.Furze, D.W.Wright, J.Gor, R.Wallis, S.J.Perkins, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.34 / 2.58
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	66.930, 98.300, 121.410, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 24.1

The binding sites of Calcium atom in the The CUB1-Egf-CUB2 Domains of Rat Mbl-Associated Serine Protease-2 (Masp-2) Bound to CA2+ (pdb code 5cis). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the The CUB1-Egf-CUB2 Domains of Rat Mbl-Associated Serine Protease-2 (Masp-2) Bound to CA2+, PDB code: 5cis:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the The CUB1-Egf-CUB2 Domains of Rat Mbl-Associated Serine Protease-2 (Masp-2) Bound to CA2+


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The CUB1-Egf-CUB2 Domains of Rat Mbl-Associated Serine Protease-2 (Masp-2) Bound to CA2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:61.6 occ:1.00 OD1 A:ASP101 2.3 47.2 1.0 OD2 A:ASP56 2.4 67.2 1.0 O A:SER103 2.4 60.1 1.0 OE1 A:GLU48 2.5 61.4 1.0 OD1 A:ASN104 2.6 74.5 1.0 O A:HOH408 2.6 70.4 1.0 OD1 A:ASP56 2.7 58.7 1.0 ND2 A:ASN104 2.7 75.9 1.0 CG A:ASN104 2.8 69.1 1.0 CG A:ASP56 2.9 59.4 1.0 C A:SER103 3.4 60.6 1.0 CG A:ASP101 3.4 53.9 1.0 CD A:GLU48 3.6 61.3 1.0 CB A:ASN104 3.9 56.2 1.0 CA A:ASN104 4.0 56.0 1.0 N A:ASN104 4.0 59.4 1.0 N A:ASP101 4.0 50.5 1.0 OD2 A:ASP101 4.1 62.2 1.0 CB A:GLU48 4.2 53.6 1.0 N A:SER103 4.3 59.7 1.0 CB A:ASP56 4.4 44.1 1.0 OE2 A:GLU48 4.4 64.2 1.0 OD1 A:ASN22 4.4 48.8 1.0 CA A:SER103 4.4 57.8 1.0 OH A:TYR20 4.5 41.2 1.0 CG A:GLU48 4.5 55.4 1.0 CB A:ASP101 4.6 47.0 1.0 C A:ASP101 4.6 49.7 1.0 CA A:ASP101 4.6 44.6 1.0 O A:ASP101 4.6 46.4 1.0 CB A:SER100 4.8 47.7 1.0 CE1 A:TYR20 4.8 54.4 1.0 C A:SER100 4.9 50.4 1.0 CA A:SER100 5.0 48.2 1.0

Calcium binding site 2 out of 3 in the The CUB1-Egf-CUB2 Domains of Rat Mbl-Associated Serine Protease-2 (Masp-2) Bound to CA2+


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The CUB1-Egf-CUB2 Domains of Rat Mbl-Associated Serine Protease-2 (Masp-2) Bound to CA2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca302 b:44.6 occ:1.00 OD1 A:ASN139 2.4 44.2 1.0 O A:VAL120 2.4 43.8 1.0 O A:HOH415 2.5 32.7 1.0 O A:TYR140 2.5 30.9 1.0 O A:GLY143 2.6 41.9 1.0 OD1 A:ASP119 2.6 28.0 1.0 OE1 A:GLU122 2.7 37.6 1.0 N A:GLY143 3.2 30.7 1.0 OD2 A:ASP119 3.2 43.7 1.0 CG A:ASP119 3.3 37.9 1.0 C A:GLY143 3.4 37.4 1.0 CG A:ASN139 3.5 44.8 1.0 CD A:GLU122 3.5 43.1 1.0 OE2 A:GLU122 3.6 38.4 1.0 C A:VAL120 3.6 29.0 1.0 C A:TYR140 3.6 28.0 1.0 CA A:GLY143 3.7 30.1 1.0 N A:GLY142 3.8 29.0 1.0 N A:TYR140 3.9 32.4 1.0 ND2 A:ASN139 4.0 37.2 1.0 C A:GLY142 4.1 34.6 1.0 N A:VAL120 4.4 31.4 1.0 CA A:GLY142 4.4 29.2 1.0 CA A:TYR140 4.4 28.1 1.0 CA A:VAL120 4.5 31.7 1.0 O A:GLY35 4.5 40.9 1.0 N A:ASP121 4.5 29.9 1.0 N A:TYR144 4.5 33.2 1.0 CA A:ASP121 4.6 37.0 1.0 C A:LEU141 4.6 32.8 1.0 N A:LEU141 4.6 30.3 1.0 N A:GLU122 4.6 40.8 1.0 CB A:ASN139 4.7 27.6 1.0 CA A:LEU141 4.7 34.6 1.0 CB A:ASP119 4.7 33.7 1.0 C A:ASN139 4.8 33.8 1.0 CA A:ASN139 4.9 33.2 1.0 C A:ASP119 4.9 37.5 1.0 CB A:VAL120 4.9 31.0 1.0 CB A:TYR144 4.9 34.7 1.0 CG A:GLU122 5.0 43.7 1.0

Calcium binding site 3 out of 3 in the The CUB1-Egf-CUB2 Domains of Rat Mbl-Associated Serine Protease-2 (Masp-2) Bound to CA2+


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of The CUB1-Egf-CUB2 Domains of Rat Mbl-Associated Serine Protease-2 (Masp-2) Bound to CA2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca303 b:45.4 occ:1.00 OD1 A:ASP262 2.3 71.0 1.0 OE2 A:GLU215 2.4 62.2 1.0 O A:HOH423 2.5 50.8 1.0 OD2 A:ASP225 2.6 52.8 1.0 O A:SER264 2.6 49.0 1.0 OD1 A:ASP225 2.8 43.5 1.0 CG A:ASP225 3.0 48.3 1.0 CG A:ASP262 3.1 62.3 1.0 OD2 A:ASP262 3.4 66.1 1.0 CD A:GLU215 3.6 55.2 1.0 C A:SER264 3.6 50.4 1.0 O A:HOH447 4.1 38.7 1.0 N A:ASP262 4.1 46.7 1.0 CB A:GLU215 4.1 43.3 1.0 CE1 A:TYR186 4.2 44.4 1.0 OH A:TYR186 4.2 44.5 1.0 CA A:GLY265 4.2 59.2 1.0 N A:GLY265 4.3 53.4 1.0 CB A:ASP262 4.4 53.5 1.0 OE1 A:GLU215 4.4 51.6 1.0 CG A:GLU215 4.5 47.4 1.0 N A:SER264 4.5 56.4 1.0 CB A:ASP225 4.5 45.7 1.0 O A:HOH410 4.6 60.9 1.0 CA A:ASP262 4.7 50.3 1.0 CZ A:TYR186 4.7 42.5 1.0 CA A:SER264 4.7 52.6 1.0 O A:HOH452 4.7 34.5 1.0 ND1 A:HIS267 4.7 43.3 1.0 C A:ASP262 4.8 50.9 1.0 CB A:THR261 5.0 49.7 1.0

R.Nan, C.M.Furze, D.W.Wright, J.Gor, R.Wallis, S.J.Perkins. Flexibility in Mannan-Binding Lectin-Associated Serine Proteases-1 and -2 Provides Insight on Lectin Pathway Activation. Structure V. 25 364 2017.
ISSN: ISSN 1878-4186
PubMed: 28111019
DOI: 10.1016/J.STR.2016.12.014