Calcium in PDB 3k21: Crystal Structure of Carboxy-Terminus of PFC0420W.

All present enzymatic activity of Crystal Structure of Carboxy-Terminus of PFC0420W.:
2.7.11.1;

The structure of Crystal Structure of Carboxy-Terminus of PFC0420W., PDB code: 3k21 was solved by A.K.Wernimont, A.Hutchinson, J.D.Artz, F.Mackenzie, D.Cossar, I.Kozieradzki, C.H.Arrowsmith, A.M.Edwards, C.Bountra, J.Weigelt, A.Bochkarev, R.Hui, M.Amani, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	16.73 / 1.15
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	50.469, 50.469, 108.656, 90.00, 90.00, 120.00
R / Rfree (%)	15 / 18.6

The binding sites of Calcium atom in the Crystal Structure of Carboxy-Terminus of PFC0420W. (pdb code 3k21). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of Carboxy-Terminus of PFC0420W., PDB code: 3k21:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Crystal Structure of Carboxy-Terminus of PFC0420W.


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 Carboxy-Terminus of PFC0420W. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca192 b:11.1 occ:1.00 OD1 A:ASP97 2.2 11.4 1.0 O A:HOH226 2.3 18.0 1.0 OD1 A:ASP99 2.4 15.1 1.0 O A:LYS103 2.4 12.0 1.0 OE1 A:GLU108 2.4 12.2 1.0 OE2 A:GLU108 2.5 12.7 1.0 OG A:SER101 2.5 14.3 1.0 CD A:GLU108 2.8 10.8 1.0 CG A:ASP99 3.3 15.9 1.0 CG A:ASP97 3.4 10.8 1.0 CB A:SER101 3.5 16.0 1.0 OD2 A:ASP99 3.6 19.8 1.0 C A:LYS103 3.6 10.3 1.0 N A:SER101 3.9 14.7 1.0 CA A:SER101 4.2 14.9 1.0 OD2 A:ASP97 4.2 13.3 1.0 CA A:ASP97 4.2 8.5 1.0 CB A:ASP97 4.3 9.2 1.0 CG A:GLU108 4.3 9.9 1.0 N A:LYS103 4.3 11.9 1.0 O A:HOH365 4.4 61.8 1.0 O A:HOH355 4.4 21.0 1.0 CA A:ILE104 4.4 8.5 0.5 N A:ASP105 4.4 9.3 1.0 CA A:ILE104 4.5 9.0 0.5 N A:ILE104 4.5 9.5 1.0 C A:ASP97 4.5 10.5 1.0 N A:ASP99 4.5 12.6 1.0 CB A:ASP99 4.5 15.1 1.0 OD2 A:ASP105 4.6 26.1 1.0 O A:HOH354 4.6 27.0 1.0 N A:GLY102 4.6 14.6 1.0 CA A:LYS103 4.6 11.7 1.0 N A:GLY100 4.6 13.4 1.0 C A:SER101 4.8 15.2 1.0 O A:HOH378 4.8 19.7 0.6 CA A:ASP99 4.9 13.6 1.0 C A:ASP99 4.9 12.6 1.0 N A:SER98 4.9 10.5 1.0 O A:ASP97 4.9 12.3 1.0 CG A:ASP105 4.9 17.3 1.0 C A:ILE104 4.9 9.3 1.0 C A:GLY100 5.0 16.9 1.0

Calcium binding site 2 out of 3 in the Crystal Structure of Carboxy-Terminus of PFC0420W.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Carboxy-Terminus of PFC0420W. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca193 b:7.3 occ:1.00 OD1 A:ASP132 2.3 8.3 1.0 O A:GLU138 2.3 10.2 1.0 OD1 A:ASP134 2.4 8.8 1.0 OD1 A:ASP136 2.4 9.0 1.0 OE1 A:GLU143 2.4 9.3 1.0 O A:HOH236 2.4 13.3 1.0 OE2 A:GLU143 2.5 9.2 1.0 CD A:GLU143 2.8 7.7 1.0 CG A:ASP134 3.3 9.2 1.0 CG A:ASP136 3.3 10.0 1.0 CG A:ASP132 3.5 6.8 1.0 C A:GLU138 3.5 7.4 1.0 OD2 A:ASP134 3.8 10.7 1.0 OD2 A:ASP136 3.8 14.8 1.0 N A:ASP136 4.1 8.9 1.0 N A:GLU138 4.2 7.8 1.0 N A:ASP134 4.3 7.4 1.0 CA A:ASP132 4.3 6.0 1.0 OD2 A:ASP132 4.3 7.8 1.0 CG A:GLU143 4.3 8.5 1.0 CA A:GLU138 4.3 7.5 0.5 CA A:GLU138 4.3 7.2 0.5 CB A:ASP136 4.3 10.9 1.0 N A:ILE139 4.4 6.6 1.0 CB A:ASP132 4.4 6.6 1.0 C A:ASP132 4.4 7.2 1.0 CB A:ASP134 4.5 8.7 1.0 CA A:ILE139 4.5 6.3 1.0 N A:ASN135 4.5 8.1 1.0 O A:HOH266 4.6 25.7 1.0 N A:VAL133 4.6 7.5 1.0 N A:THR140 4.6 7.5 1.0 CA A:ASP136 4.7 9.9 1.0 CG2 A:THR140 4.7 12.9 1.0 CA A:ASP134 4.7 7.9 1.0 CB A:GLU138 4.7 9.0 0.5 C A:ASP134 4.7 7.7 1.0 CB A:GLU138 4.7 9.3 0.5 N A:GLY137 4.8 8.3 1.0 O A:ASP132 4.9 7.3 1.0 C A:ASP136 5.0 9.7 1.0 C A:ILE139 5.0 6.8 1.0

Calcium binding site 3 out of 3 in the Crystal Structure of Carboxy-Terminus of PFC0420W.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Carboxy-Terminus of PFC0420W. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca194 b:7.5 occ:1.00 OD1 A:ASP173 2.3 9.3 1.0 O A:LYS179 2.3 8.0 1.0 OD1 A:ASN175 2.4 11.0 1.0 O A:HOH219 2.4 12.7 1.0 OD1 A:ASP177 2.4 9.4 1.0 OE1 A:GLU184 2.5 7.0 1.0 OE2 A:GLU184 2.5 8.2 1.0 CD A:GLU184 2.9 7.6 1.0 CG A:ASP177 3.3 11.0 1.0 CG A:ASN175 3.3 12.6 1.0 CG A:ASP173 3.4 9.1 1.0 C A:LYS179 3.5 6.3 1.0 OD2 A:ASP177 3.6 14.7 1.0 ND2 A:ASN175 3.8 17.1 1.0 OD2 A:ASP173 4.1 11.7 1.0 N A:LYS179 4.2 7.9 1.0 N A:ASN175 4.3 11.5 1.0 CB A:ASP173 4.3 11.6 1.0 CA A:LYS179 4.3 7.2 1.0 CG A:GLU184 4.4 6.9 1.0 N A:ILE180 4.4 5.8 1.0 CA A:ASP173 4.4 8.9 1.0 N A:LYS174 4.4 9.3 0.5 CA A:ILE180 4.4 5.7 1.0 N A:LYS174 4.5 9.9 0.5 N A:ASP177 4.5 12.3 1.0 N A:ASP181 4.5 5.8 1.0 CB A:ASP177 4.5 13.3 1.0 CB A:ASN175 4.6 15.0 1.0 CB A:LYS179 4.7 9.5 1.0 CA A:ASN175 4.8 13.2 1.0 N A:ASN176 4.8 14.5 0.5 N A:ASN176 4.8 15.1 0.5 OE1 A:GLU138 4.8 7.3 0.5 CA A:ASP177 4.8 12.3 1.0 N A:GLY178 4.9 9.5 1.0 C A:ASN175 4.9 14.8 1.0 C A:ILE180 4.9 5.3 1.0 C A:ASP173 4.9 9.8 1.0 OD2 A:ASP181 4.9 12.5 1.0 CG A:ASP181 5.0 8.2 1.0

A.K.Wernimont, M.Amani, W.Qiu, J.C.Pizarro, J.D.Artz, Y.H.Lin, J.Lew, A.Hutchinson, R.Hui. Structures of Parasitic Cdpk Domains Point to A Common Mechanism of Activation. Proteins V. 79 803 2011.
ISSN: ISSN 0887-3585
PubMed: 21287613
DOI: 10.1002/PROT.22919