Calcium in PDB 4wpa: Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium

All present enzymatic activity of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium:
4.6.1.1;

The structure of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium, PDB code: 4wpa was solved by N.G.Bharambe, D.V.Barathy, K.Suguna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.99 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.720, 55.720, 55.330, 90.00, 110.22, 90.00
R / Rfree (%)	18.8 / 22.4

The binding sites of Calcium atom in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium (pdb code 4wpa). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium, PDB code: 4wpa:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium


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 Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:18.6 occ:1.00 OD2 A:ASP105 2.3 18.0 1.0 O21 A:PPV302 2.3 19.3 1.0 OD1 A:ASP61 2.4 20.6 1.0 O A:ILE62 2.4 19.0 1.0 O A:HOH465 2.4 31.6 1.0 O12 A:PPV302 2.4 16.0 1.0 HH12 A:ARG143 3.2 31.3 1.0 CG A:ASP105 3.4 20.4 1.0 P2 A:PPV302 3.4 18.9 1.0 CG A:ASP61 3.5 33.5 1.0 HG A:SER65 3.5 21.4 1.0 C A:ILE62 3.5 19.4 1.0 P1 A:PPV302 3.5 19.4 1.0 HB2 A:ASP61 3.5 31.2 1.0 O22 A:PPV302 3.7 20.5 1.0 OD1 A:ASP105 3.7 28.2 1.0 H A:SER65 3.7 23.8 1.0 H A:ILE62 3.8 19.7 1.0 OPP A:PPV302 3.8 20.4 1.0 O A:HOH430 3.9 48.9 1.0 N A:ILE62 3.9 16.4 1.0 NH1 A:ARG143 4.0 26.1 1.0 HB3 A:SER65 4.0 21.6 1.0 CB A:ASP61 4.0 26.0 1.0 H A:GLU64 4.1 26.9 1.0 OG A:SER65 4.1 17.9 1.0 O11 A:PPV302 4.1 15.8 1.0 HH11 A:ARG143 4.2 31.3 1.0 HA A:GLU63 4.2 24.0 1.0 HB A:ILE62 4.2 25.4 1.0 CA A:ILE62 4.2 16.3 1.0 C A:ASP61 4.4 14.5 1.0 OD2 A:ASP61 4.5 24.4 1.0 N A:GLU63 4.5 18.1 1.0 CB A:SER65 4.5 18.0 1.0 N A:GLU64 4.6 22.4 1.0 O31 A:PPV302 4.6 25.9 1.0 O A:HOH548 4.6 31.2 1.0 N A:SER65 4.6 19.8 1.0 O32 A:PPV302 4.6 22.3 1.0 CB A:ASP105 4.7 19.8 1.0 HB2 A:ASP105 4.7 23.8 1.0 CA A:GLU63 4.7 20.0 1.0 HH22 A:ARG143 4.7 43.5 1.0 HB3 A:ASP61 4.8 31.2 1.0 CB A:ILE62 4.8 21.1 1.0 CA A:ASP61 4.9 18.6 1.0 C A:GLU63 4.9 22.0 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium


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 Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca301 b:18.2 occ:1.00 OD2 B:ASP105 2.3 20.3 1.0 O21 B:PPV302 2.3 22.6 1.0 OD2 B:ASP61 2.3 26.9 1.0 O22 B:PPV302 2.4 16.1 1.0 O B:ILE62 2.4 16.4 1.0 O B:HOH531 2.4 33.5 1.0 HH12 B:ARG143 3.0 59.5 1.0 HB2 B:ASP61 3.4 21.3 1.0 CG B:ASP105 3.4 28.5 1.0 P2 B:PPV302 3.4 18.6 1.0 CG B:ASP61 3.4 26.6 1.0 HG B:SER65 3.5 17.0 1.0 C B:ILE62 3.5 14.9 1.0 P1 B:PPV302 3.5 19.2 1.0 H B:ILE62 3.6 20.6 1.0 NH1 B:ARG143 3.7 49.6 1.0 O12 B:PPV302 3.7 17.8 1.0 OD1 B:ASP105 3.7 24.1 1.0 HH11 B:ARG143 3.7 59.5 1.0 H B:SER65 3.7 18.5 0.6 H B:SER65 3.7 18.5 0.4 OPP B:PPV302 3.8 18.0 1.0 N B:ILE62 3.8 17.2 1.0 O B:HOH423 3.9 43.6 1.0 CB B:ASP61 3.9 17.8 1.0 HB3 B:SER65 3.9 16.7 1.0 OG B:SER65 4.0 14.2 1.0 O B:HOH511 4.1 47.0 1.0 HA B:GLU63 4.2 20.1 1.0 CA B:ILE62 4.2 16.2 1.0 H B:GLU64 4.3 20.1 0.4 O31 B:PPV302 4.3 18.1 1.0 C B:ASP61 4.3 15.7 1.0 H B:GLU64 4.3 21.1 0.6 HB B:ILE62 4.4 18.2 1.0 OD1 B:ASP61 4.4 26.0 1.0 CB B:SER65 4.5 13.9 1.0 N B:GLU63 4.5 15.9 1.0 N B:SER65 4.6 15.4 1.0 O11 B:PPV302 4.6 18.2 1.0 HB2 B:ASP105 4.6 25.7 1.0 CB B:ASP105 4.6 21.4 1.0 HB3 B:ASP61 4.7 21.3 1.0 N B:GLU64 4.7 16.8 0.4 N B:GLU64 4.7 17.6 0.6 CA B:GLU63 4.7 16.7 1.0 CA B:ASP61 4.7 16.7 1.0 O32 B:PPV302 4.7 17.2 1.0 HH22 B:ARG143 4.8 39.5 1.0 CB B:ILE62 4.9 15.2 1.0 CZ B:ARG143 4.9 37.0 1.0 C B:GLU63 4.9 20.4 1.0 O B:ASP61 5.0 15.1 1.0

D.V.Barathy, N.G.Bharambe, W.Syed, A.Zaveri, S.S.Visweswariah, M.Cola Sigmaf O, S.Misquith, K.Suguna. Autoinhibitory Mechanism and Activity-Related Structural Changes in A Mycobacterial Adenylyl Cyclase J.Struct.Biol. V. 190 304 2015.
ISSN: ESSN 1095-8657
PubMed: 25916753
DOI: 10.1016/J.JSB.2015.04.013