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Calcium in PDB 4usu: Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate

Enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate

All present enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate:
4.6.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate, PDB code: 4usu was solved by S.Kleinboelting, C.Steegborn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 64.83 / 1.95
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 100.840, 100.840, 96.770, 90.00, 90.00, 120.00
R / Rfree (%) 15.93 / 21.174

Other elements in 4usu:

The structure of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate (pdb code 4usu). 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 Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate, PDB code: 4usu:

Calcium binding site 1 out of 1 in 4usu

Go back to Calcium Binding Sites List in 4usu
Calcium binding site 1 out of 1 in the Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate


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 Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1471

b:52.4
occ:1.00
 O2G A:APC1470 2.4 34.5 1.0
OD1 A:ASP99 2.4 34.4 1.0
OD1 A:ASP47 2.4 39.4 1.0
O A:HOH2036 2.5 43.3 1.0
O1B A:APC1470 2.5 41.3 1.0
O A:ILE48 2.6 36.0 1.0
CG A:ASP99 3.1 32.3 1.0
CG A:ASP47 3.3 46.0 1.0
OD2 A:ASP99 3.4 37.1 1.0
OD2 A:ASP47 3.4 50.5 1.0
PB A:APC1470 3.4 42.8 1.0
O A:HOH2076 3.5 34.8 1.0
PG A:APC1470 3.7 37.4 1.0
O3B A:APC1470 3.7 40.9 1.0
C A:ILE48 3.7 42.3 1.0
O1A A:APC1470 4.0 45.1 1.0
C3A A:APC1470 4.0 48.7 1.0
O A:HOH2074 4.3 36.5 1.0
N A:ILE48 4.4 40.0 1.0
CB A:ASP99 4.4 32.0 1.0
N A:SER49 4.6 38.9 1.0
O3G A:APC1470 4.6 37.0 1.0
CA A:ILE48 4.6 43.7 1.0
C A:ASP99 4.6 29.2 1.0
O1G A:APC1470 4.7 35.1 1.0
CB A:ASP47 4.7 42.8 1.0
CA A:SER49 4.7 44.8 1.0
C A:ASP47 4.7 40.2 1.0
PA A:APC1470 4.7 55.2 1.0
O A:ASP99 4.7 30.7 1.0
O2B A:APC1470 4.7 42.0 1.0
O A:HOH2071 4.8 37.1 1.0
CA A:ASP99 4.9 30.0 1.0
CB A:ALA100 4.9 28.5 1.0
N A:ALA100 4.9 33.0 1.0
CA A:ASP47 5.0 38.3 1.0

Reference:

S.Kleinbolting, J.Van Den Heuvel, C.Steegborn. Structural Analysis of Human Soluble Adenylyl Cyclase and Crystal Structures of Its Nucleotide Complexes - Implications For Cyclase Catalysis and Evolution. Febs J. V. 281 4151 2014.
ISSN: ISSN 1742-464X
PubMed: 25040695
DOI: 10.1111/FEBS.12913
Page generated: Wed Jul 9 02:24:45 2025

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