Potassium in PDB 2qki: Human C3C in Complex with the Inhibitor Compstatin

The structure of Human C3C in Complex with the Inhibitor Compstatin, PDB code: 2qki was solved by B.J.C.Janssen, E.F.Halff, J.D.Lambris, P.Gros, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.00 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	85.809, 124.754, 127.367, 90.00, 95.08, 90.00
R / Rfree (%)	21.3 / 28.1

The structure of Human C3C in Complex with the Inhibitor Compstatin also contains other interesting chemical elements:

Bromine

(Br)

32 atoms

The binding sites of Potassium atom in the Human C3C in Complex with the Inhibitor Compstatin (pdb code 2qki). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 5 binding sites of Potassium where determined in the Human C3C in Complex with the Inhibitor Compstatin, PDB code: 2qki:
Jump to Potassium binding site number: 1; 2; 3; 4; 5;

Potassium binding site 1 out of 5 in the Human C3C in Complex with the Inhibitor Compstatin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human C3C in Complex with the Inhibitor Compstatin within 5.0Å range: probe atom residue distance (Å) B Occ A:K3002 b:57.8 occ:1.00 O A:VAL533 2.6 42.0 1.0 O A:PRO505 2.8 35.2 1.0 OD1 A:ASP535 2.9 47.5 1.0 OD1 A:ASP532 3.0 46.0 1.0 OD2 A:ASP532 3.3 44.6 1.0 CG A:ASP532 3.4 43.3 1.0 CG A:ASP535 3.6 46.8 1.0 C A:PRO505 3.8 35.2 1.0 C A:VAL533 3.8 42.0 1.0 O A:HOH3106 3.8 51.4 1.0 OD2 A:ASP535 4.1 47.8 1.0 CA A:PRO505 4.1 35.4 1.0 N A:VAL533 4.1 40.7 1.0 N A:ASP535 4.2 45.0 1.0 CA A:VAL533 4.6 41.1 1.0 C A:LYS534 4.6 44.5 1.0 CB A:ASP535 4.7 46.1 1.0 N A:LYS534 4.7 42.6 1.0 CA A:LYS534 4.7 43.9 1.0 CA A:ASP535 4.8 45.8 1.0 CB A:ASP532 4.8 40.9 1.0 CB A:PRO505 4.9 35.1 1.0 N A:SER506 5.0 35.0 1.0

Potassium binding site 2 out of 5 in the Human C3C in Complex with the Inhibitor Compstatin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Human C3C in Complex with the Inhibitor Compstatin within 5.0Å range: probe atom residue distance (Å) B Occ C:K602 b:64.3 occ:1.00 O C:HOH522 2.7 76.3 1.0 O C:ARG1405 2.8 47.5 1.0 O C:GLY1402 2.9 49.4 1.0 O C:ALA1400 2.9 47.4 1.0 C C:GLY1402 3.8 49.4 1.0 C C:ARG1405 4.0 47.7 1.0 C C:ALA1400 4.1 47.3 1.0 N C:ARG1405 4.3 48.8 1.0 C C:ASN1401 4.3 48.3 1.0 N C:GLY1402 4.4 48.7 1.0 CA C:ASN1401 4.4 48.1 1.0 CA C:VAL1403 4.4 49.9 1.0 N C:VAL1403 4.5 49.7 1.0 N C:ASP1404 4.5 49.7 1.0 O C:ASN1401 4.7 48.3 1.0 CA C:ARG1405 4.7 48.3 1.0 N C:ASN1401 4.8 47.8 1.0 C C:VAL1403 4.8 49.9 1.0 CA C:GLY1402 4.8 49.1 1.0

Potassium binding site 3 out of 5 in the Human C3C in Complex with the Inhibitor Compstatin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Human C3C in Complex with the Inhibitor Compstatin within 5.0Å range: probe atom residue distance (Å) B Occ D:K3002 b:41.6 occ:1.00 O D:VAL533 2.6 48.9 1.0 O D:PRO505 2.6 41.6 1.0 OD1 D:ASP535 2.7 54.0 1.0 OD1 D:ASP532 2.7 47.8 1.0 O D:HOH3171 3.1 37.4 1.0 C D:VAL533 3.7 48.4 1.0 C D:PRO505 3.7 41.7 1.0 CG D:ASP535 3.8 52.4 1.0 CG D:ASP532 3.8 48.1 1.0 N D:ASP535 3.9 50.9 1.0 N D:VAL533 4.1 47.1 1.0 CA D:PRO505 4.3 41.8 1.0 OD2 D:ASP532 4.3 50.4 1.0 C D:LYS534 4.3 50.7 1.0 CA D:ASP535 4.4 50.7 1.0 CB D:ASP535 4.5 51.1 1.0 CA D:VAL533 4.5 47.6 1.0 OE2 D:GLU599 4.5 54.7 1.0 N D:LYS534 4.6 49.6 1.0 CA D:LYS534 4.6 50.4 1.0 OD2 D:ASP535 4.7 54.8 1.0 CB D:PRO505 4.8 41.4 1.0 N D:SER506 4.8 42.0 1.0 O D:LYS534 4.9 51.1 1.0 C D:ASP532 5.0 46.4 1.0

Potassium binding site 4 out of 5 in the Human C3C in Complex with the Inhibitor Compstatin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Human C3C in Complex with the Inhibitor Compstatin within 5.0Å range: probe atom residue distance (Å) B Occ D:K3003 b:80.5 occ:1.00 NH2 D:ARG13 2.8 44.2 1.0 O D:ALA601 2.8 43.1 1.0 C D:ALA601 3.4 43.6 1.0 O D:LYS475 3.5 41.0 1.0 C D:LYS475 3.7 41.4 1.0 CZ D:ARG13 3.7 46.1 1.0 NH1 D:ARG13 3.8 47.4 1.0 CB D:ALA601 3.9 42.8 1.0 N D:ASP602 4.0 44.3 1.0 CA D:ASP602 4.1 45.2 1.0 N D:GLY476 4.1 41.7 1.0 OH D:TYR107 4.1 44.9 1.0 CA D:GLY476 4.2 42.2 1.0 CA D:ALA601 4.3 43.4 1.0 CA D:LYS475 4.3 41.1 1.0 O D:VAL598 4.4 42.3 1.0 N D:ILE603 4.6 44.8 1.0 C D:ASP602 4.7 45.1 1.0 CG2 D:ILE603 4.8 43.4 1.0 BR D:BR703 4.8 54.0 0.8 CB D:HIS132 4.9 44.0 1.0 NE D:ARG13 5.0 46.3 1.0

Potassium binding site 5 out of 5 in the Human C3C in Complex with the Inhibitor Compstatin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Human C3C in Complex with the Inhibitor Compstatin within 5.0Å range: probe atom residue distance (Å) B Occ F:K605 b:51.1 occ:1.00 O F:ARG1405 2.7 39.6 1.0 O F:GLY1402 2.8 43.6 1.0 O F:ALA1400 2.9 44.7 1.0 C F:ARG1405 3.8 40.1 1.0 C F:GLY1402 3.9 43.5 1.0 O F:ASN1401 4.0 43.6 1.0 C F:ALA1400 4.1 44.3 1.0 C F:ASN1401 4.1 43.8 1.0 O F:VAL1403 4.3 43.2 1.0 N F:ARG1405 4.4 41.4 1.0 CA F:ASN1401 4.5 44.1 1.0 N F:GLY1402 4.5 43.6 1.0 C F:VAL1403 4.6 43.0 1.0 CA F:ARG1405 4.6 40.8 1.0 CA F:VAL1403 4.7 43.1 1.0 N F:ASN1401 4.7 44.2 1.0 N F:VAL1403 4.8 43.4 1.0 N F:TYR1406 4.8 39.8 1.0 CA F:GLY1402 4.8 43.7 1.0 CA F:TYR1406 4.9 38.9 1.0

B.J.Janssen, E.F.Halff, J.D.Lambris, P.Gros. Structure of Compstatin in Complex with Complement Component C3C Reveals A New Mechanism of Complement Inhibition. J.Biol.Chem. V. 282 29241 2007.
ISSN: ISSN 0021-9258
PubMed: 17684013
DOI: 10.1074/JBC.M704587200