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Calcium in PDB 3pak: Crystal Structure of Rat Surfactant Protein A Neck and Carbohydrate Recognition Domain (Ncrd) Complexed with Mannose

Protein crystallography data

The structure of Crystal Structure of Rat Surfactant Protein A Neck and Carbohydrate Recognition Domain (Ncrd) Complexed with Mannose, PDB code: 3pak was solved by F.Shang, M.J.Rynkiewicz, F.X.Mccormack, H.Wu, T.M.Cafarella, J.Head, B.A.Seaton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.10 / 1.90
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 97.796, 97.796, 45.088, 90.00, 90.00, 120.00
R / Rfree (%) 21.8 / 24.3

Other elements in 3pak:

The structure of Crystal Structure of Rat Surfactant Protein A Neck and Carbohydrate Recognition Domain (Ncrd) Complexed with Mannose also contains other interesting chemical elements:

Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Rat Surfactant Protein A Neck and Carbohydrate Recognition Domain (Ncrd) Complexed with Mannose (pdb code 3pak). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Rat Surfactant Protein A Neck and Carbohydrate Recognition Domain (Ncrd) Complexed with Mannose, PDB code: 3pak:

Calcium binding site 1 out of 1 in 3pak

Go back to Calcium Binding Sites List in 3pak
Calcium binding site 1 out of 1 in the Crystal Structure of Rat Surfactant Protein A Neck and Carbohydrate Recognition Domain (Ncrd) Complexed with Mannose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Rat Surfactant Protein A Neck and Carbohydrate Recognition Domain (Ncrd) Complexed with Mannose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca300

b:34.2
occ:1.00
OD1 A:ASP215 2.3 37.2 1.0
O4 A:MAN500 2.3 49.3 1.0
OD1 A:ASN214 2.3 33.3 1.0
O3 A:MAN500 2.4 49.5 1.0
O A:ASP215 2.4 30.0 1.0
OE1 A:GLU195 2.4 30.0 1.0
O A:HOH518 2.5 48.1 1.0
OE1 A:GLU202 2.7 42.5 1.0
C3 A:MAN500 3.1 53.4 1.0
C4 A:MAN500 3.1 53.6 1.0
CG A:ASP215 3.2 36.5 1.0
CD A:GLU195 3.3 30.7 1.0
CG A:ASN214 3.4 33.0 1.0
C A:ASP215 3.5 32.0 1.0
CD A:GLU202 3.6 41.0 1.0
N A:ASP215 3.6 31.8 1.0
OE2 A:GLU195 3.7 31.0 1.0
ND2 A:ASN214 3.9 32.5 1.0
OD2 A:ASP215 3.9 38.2 1.0
OE2 A:GLU202 4.0 39.9 1.0
CA A:ASP215 4.0 32.1 1.0
CB A:ASP215 4.2 33.5 1.0
C A:ASN214 4.4 31.0 1.0
N A:ARG197 4.4 37.2 1.0
N A:GLY198 4.4 44.8 1.0
C5 A:MAN500 4.5 55.0 1.0
C2 A:MAN500 4.5 55.5 1.0
CG A:GLU195 4.6 28.9 1.0
CB A:ASN214 4.6 30.4 1.0
N A:ARG216 4.7 32.2 1.0
CA A:ASN214 4.7 30.1 1.0
CA A:GLY198 4.7 46.9 1.0
C A:ARG197 4.8 43.5 1.0
CG A:ARG197 4.8 43.6 1.0
CG A:GLU202 4.9 42.7 1.0
O2 A:MAN500 4.9 56.0 1.0

Reference:

F.Shang, M.J.Rynkiewicz, F.X.Mccormack, H.Wu, T.M.Cafarella, J.F.Head, B.A.Seaton. Crystallographic Complexes of Surfactant Protein A and Carbohydrates Reveal Ligand-Induced Conformational Change. J.Biol.Chem. V. 286 757 2011.
ISSN: ISSN 0021-9258
PubMed: 21047777
DOI: 10.1074/JBC.M110.175265
Page generated: Sat Jul 13 16:40:19 2024

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