Calcium in PDB 9fmu: Cryo-Em Structure of Human CD163 SRCR1-9 in Complex with Haptoglobin- Hemoglobin

The structure of Cryo-Em Structure of Human CD163 SRCR1-9 in Complex with Haptoglobin- Hemoglobin also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Calcium atom in the Cryo-Em Structure of Human CD163 SRCR1-9 in Complex with Haptoglobin- Hemoglobin (pdb code 9fmu). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Cryo-Em Structure of Human CD163 SRCR1-9 in Complex with Haptoglobin- Hemoglobin, PDB code: 9fmu:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Cryo-Em Structure of Human CD163 SRCR1-9 in Complex with Haptoglobin- Hemoglobin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cryo-Em Structure of Human CD163 SRCR1-9 in Complex with Haptoglobin- Hemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca2001 b:250.3 occ:1.00 OD2 D:ASP225 2.0 247.9 1.0 CG D:ASP225 2.4 247.9 1.0 OD2 D:ASP224 2.4 247.2 1.0 ND2 D:ASN247 2.4 225.3 1.0 OD1 D:ASP224 2.5 247.2 1.0 OD1 D:ASN247 2.5 225.3 1.0 OD1 D:ASP225 2.6 247.9 1.0 CG D:ASN247 2.7 225.3 1.0 CG D:ASP224 2.7 247.2 1.0 OD2 D:ASP186 2.9 231.2 1.0 CB D:ASP225 3.6 247.9 1.0 CG D:ASP186 3.7 231.2 1.0 N D:ASP225 3.9 247.9 1.0 SG D:CYS248 4.1 233.7 1.0 CB D:ASP186 4.1 231.2 1.0 CB D:ASN247 4.1 225.3 1.0 NZ C:LYS321 4.1 201.2 1.0 CB D:ASP224 4.2 247.2 1.0 CA D:ASP225 4.2 247.9 1.0 N D:ASN247 4.4 225.3 1.0 OD1 D:ASP186 4.5 231.2 1.0 C D:ASP224 4.6 247.2 1.0 CA D:ASN247 4.8 225.3 1.0 CA D:ASP224 4.9 247.2 1.0 CE C:LYS321 4.9 201.2 1.0

Calcium binding site 2 out of 3 in the Cryo-Em Structure of Human CD163 SRCR1-9 in Complex with Haptoglobin- Hemoglobin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Cryo-Em Structure of Human CD163 SRCR1-9 in Complex with Haptoglobin- Hemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca2002 b:196.5 occ:1.00 O D:GLY294 2.1 162.0 1.0 OD2 D:ASP299 2.3 168.8 1.0 O D:VAL333 2.3 176.6 1.0 C D:GLY294 3.2 162.0 1.0 CG D:ASP299 3.3 168.8 1.0 N D:ASP296 3.3 162.3 1.0 C D:VAL333 3.5 176.6 1.0 OD1 D:ASP299 3.6 168.8 1.0 CG D:ASP296 3.6 162.3 1.0 CA D:TRP295 3.7 163.2 1.0 OD2 D:ASP296 3.7 162.3 1.0 CA D:SER334 3.7 181.2 1.0 N D:TRP295 3.8 163.2 1.0 C D:TRP295 3.8 163.2 1.0 CB D:SER334 3.9 181.2 1.0 CB D:ASP296 3.9 162.3 1.0 OD1 D:ASP296 4.0 162.3 1.0 N D:SER334 4.1 181.2 1.0 CA D:ASP296 4.2 162.3 1.0 CA D:GLY294 4.3 162.0 1.0 CB D:ASP299 4.6 168.8 1.0 CA D:VAL333 4.7 176.6 1.0 CG1 D:VAL333 4.7 176.6 1.0 N D:VAL333 4.8 176.6 1.0 O D:TRP295 4.9 163.2 1.0

Calcium binding site 3 out of 3 in the Cryo-Em Structure of Human CD163 SRCR1-9 in Complex with Haptoglobin- Hemoglobin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Cryo-Em Structure of Human CD163 SRCR1-9 in Complex with Haptoglobin- Hemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ E:Ca1101 b:302.8 occ:1.00 OD2 E:ASP299 2.3 322.7 1.0 O E:GLY294 2.3 299.9 1.0 O E:VAL333 2.4 305.5 1.0 CG E:ASP299 3.2 322.7 1.0 OD2 E:ASP296 3.3 315.9 1.0 CA E:SER334 3.3 309.8 1.0 OD1 E:ASP299 3.4 322.7 1.0 C E:VAL333 3.4 305.5 1.0 CG E:ASP296 3.4 315.9 1.0 C E:GLY294 3.5 299.9 1.0 N E:ASP296 3.8 315.9 1.0 N E:SER334 3.8 309.8 1.0 CB E:ASP296 3.8 315.9 1.0 OD1 E:ASP296 3.9 315.9 1.0 CB E:SER334 4.0 309.8 1.0 CA E:TRP295 4.3 322.9 1.0 N E:CYS335 4.3 321.0 1.0 N E:TRP295 4.3 322.9 1.0 C E:TRP295 4.3 322.9 1.0 C E:SER334 4.3 309.8 1.0 CA E:GLY294 4.4 299.9 1.0 CA E:ASP296 4.4 315.9 1.0 CB E:ASP299 4.6 322.7 1.0 CG2 E:VAL333 4.7 305.5 1.0 CA E:VAL333 4.7 305.5 1.0

A.Etzerodt, J.H.Mikkelsen, M.Torvund-Jensen, D.Hennig, T.Boesen, J.H.Graversen, S.K.Moestrup, J.M.Kollman, C.B.F.Andersen. The Structure of Human Scavenger Receptor CD163 in Complex with Haptoglobin-Hemoglobin Discloses the Molecular Mechanism For Hemoglobin Scavenging. To Be Published.