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

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

All present enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate Soaked with Bisulfite:
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 Soaked with Bisulfite, PDB code: 4clw was solved by S.Kleinboelting, M.Weyand, C.Steegborn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 87.10 / 2.15
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 100.570, 100.570, 97.170, 90.00, 90.00, 120.00
R / Rfree (%) 16.211 / 20.289

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 Soaked with Bisulfite (pdb code 4clw). 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 Soaked with Bisulfite, PDB code: 4clw:

Calcium binding site 1 out of 1 in 4clw

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


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 Soaked with Bisulfite within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1474

b:70.8
occ:1.00
 O A:HOH2027 2.4 51.0 1.0
O1G A:APC1467 2.4 54.7 1.0
OD1 A:ASP47 2.4 60.3 1.0
OD1 A:ASP99 2.4 45.0 1.0
O1B A:APC1467 2.5 52.1 1.0
O A:ILE48 2.6 52.5 1.0
CG A:ASP99 3.1 52.2 1.0
OD2 A:ASP99 3.3 50.2 1.0
CG A:ASP47 3.4 57.1 1.0
O A:HOH2057 3.5 44.1 1.0
PB A:APC1467 3.5 57.2 1.0
OD2 A:ASP47 3.6 53.9 1.0
PG A:APC1467 3.7 55.8 1.0
C A:ILE48 3.7 53.2 1.0
O3B A:APC1467 3.7 55.2 1.0
C3A A:APC1467 4.1 57.4 1.0
O2A A:APC1467 4.2 58.2 1.0
N A:ILE48 4.3 47.0 1.0
CB A:ASP99 4.4 49.0 1.0
O A:HOH2056 4.5 58.3 1.0
N A:SER49 4.6 46.9 1.0
CA A:ILE48 4.6 51.8 1.0
O2G A:APC1467 4.6 50.8 1.0
O A:ASP99 4.6 41.3 1.0
C A:ASP99 4.6 42.8 1.0
CA A:SER49 4.7 58.2 1.0
O3G A:APC1467 4.7 53.4 1.0
CB A:ASP47 4.8 50.8 1.0
O2B A:APC1467 4.8 61.6 1.0
PA A:APC1467 4.9 67.1 1.0
O A:HOH2054 4.9 53.9 1.0
C A:ASP47 4.9 47.5 1.0
CA A:ASP99 4.9 45.2 1.0
CB A:ALA100 4.9 34.9 1.0
N A:ALA100 5.0 40.3 1.0

Reference:

S.Kleinboelting, A.Diaz, S.Moniot, J.Van Den Heuvel, M.Weyand, L.R.Levin, J.Buck, C.Steegborn. Crystal Structures of Human Soluble Adenylyl Cyclase Reveal Mechanisms of Catalysis and of Its Activation Through Bicarbonate. Proc.Natl.Acad.Sci.Usa V. 111 3727 2014.
ISSN: ISSN 0027-8424
PubMed: 24567411
DOI: 10.1073/PNAS.1322778111
Page generated: Sat Dec 12 04:42:25 2020

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