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Strontium in PDB 1wc3: Soluble Adenylyl Cyclase Cyac From S. Platensis in Complex with Alpha,Beta-Methylene-Atp and Strontium

Enzymatic activity of Soluble Adenylyl Cyclase Cyac From S. Platensis in Complex with Alpha,Beta-Methylene-Atp and Strontium

All present enzymatic activity of Soluble Adenylyl Cyclase Cyac From S. Platensis in Complex with Alpha,Beta-Methylene-Atp and Strontium:
4.6.1.1;

Protein crystallography data

The structure of Soluble Adenylyl Cyclase Cyac From S. Platensis in Complex with Alpha,Beta-Methylene-Atp and Strontium, PDB code: 1wc3 was solved by C.Steegborn, T.N.Litvin, L.R.Levin, J.Buck, H.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.0 / 1.9
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.672, 71.539, 99.572, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 23.6

Strontium Binding Sites:

The binding sites of Strontium atom in the Soluble Adenylyl Cyclase Cyac From S. Platensis in Complex with Alpha,Beta-Methylene-Atp and Strontium (pdb code 1wc3). This binding sites where shown within 5.0 Angstroms radius around Strontium atom.
In total 2 binding sites of Strontium where determined in the Soluble Adenylyl Cyclase Cyac From S. Platensis in Complex with Alpha,Beta-Methylene-Atp and Strontium, PDB code: 1wc3:
Jump to Strontium binding site number: 1; 2;

Strontium binding site 1 out of 2 in 1wc3

Go back to Strontium Binding Sites List in 1wc3
Strontium binding site 1 out of 2 in the Soluble Adenylyl Cyclase Cyac From S. Platensis in Complex with Alpha,Beta-Methylene-Atp and Strontium


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 1 of Soluble Adenylyl Cyclase Cyac From S. Platensis in Complex with Alpha,Beta-Methylene-Atp and Strontium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sr1501

b:33.7
occ:0.91
O1B A:APC1500 2.3 20.9 1.0
O A:HOH2103 2.4 21.7 1.0
OD1 A:ASP1017 2.4 25.4 1.0
O A:ILE1018 2.4 20.7 1.0
OD1 A:ASP1061 2.5 14.9 1.0
O3G A:APC1500 2.5 20.1 1.0
OD2 A:ASP1017 2.8 25.5 1.0
CG A:ASP1017 2.9 25.1 1.0
CG A:ASP1061 3.4 17.6 1.0
PB A:APC1500 3.5 25.6 1.0
C A:ILE1018 3.7 21.8 1.0
OD2 A:ASP1061 3.7 22.9 1.0
PG A:APC1500 3.7 22.8 1.0
O3B A:APC1500 3.8 21.4 1.0
C3A A:APC1500 4.0 25.1 1.0
N A:ILE1018 4.1 21.6 1.0
O1A A:APC1500 4.2 22.9 1.0
O A:HOH2030 4.2 21.9 1.0
CB A:ASP1017 4.4 23.7 1.0
CA A:ILE1018 4.5 22.6 1.0
N A:VAL1019 4.6 23.1 1.0
O A:HOH2101 4.6 41.7 1.0
CA A:VAL1019 4.6 25.4 1.0
CG2 A:VAL1019 4.6 28.8 1.0
O2G A:APC1500 4.7 19.8 1.0
O1G A:APC1500 4.7 19.9 1.0
CB A:ASP1061 4.7 17.3 1.0
O2B A:APC1500 4.8 25.2 1.0
O A:HOH2027 4.8 18.3 1.0
PA A:APC1500 4.8 26.3 1.0
C A:ASP1017 4.8 22.5 1.0
CG1 A:ILE1018 4.9 21.7 1.0
O A:HOH2099 4.9 17.6 1.0

Strontium binding site 2 out of 2 in 1wc3

Go back to Strontium Binding Sites List in 1wc3
Strontium binding site 2 out of 2 in the Soluble Adenylyl Cyclase Cyac From S. Platensis in Complex with Alpha,Beta-Methylene-Atp and Strontium


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 2 of Soluble Adenylyl Cyclase Cyac From S. Platensis in Complex with Alpha,Beta-Methylene-Atp and Strontium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Sr1501

b:33.6
occ:0.91
O3G B:APC1500 2.4 22.9 1.0
O1B B:APC1500 2.4 26.1 1.0
O B:HOH2110 2.4 22.2 1.0
O B:ILE1018 2.5 16.9 1.0
OD1 B:ASP1017 2.5 16.5 1.0
OD2 B:ASP1061 2.6 19.5 1.0
OD2 B:ASP1017 2.6 20.3 1.0
CG B:ASP1017 2.9 20.6 1.0
CG B:ASP1061 3.5 21.6 1.0
PB B:APC1500 3.6 27.7 1.0
PG B:APC1500 3.7 27.0 1.0
C B:ILE1018 3.7 19.3 1.0
OD1 B:ASP1061 3.7 21.5 1.0
O3B B:APC1500 3.8 25.6 1.0
N B:ILE1018 4.1 19.0 1.0
O1A B:APC1500 4.2 30.2 1.0
C3A B:APC1500 4.2 26.8 1.0
O B:HOH2034 4.4 25.4 1.0
CB B:ASP1017 4.4 18.0 1.0
CG2 B:VAL1019 4.5 24.9 1.0
N B:VAL1019 4.6 19.2 1.0
CA B:ILE1018 4.6 18.7 1.0
CA B:VAL1019 4.6 21.7 1.0
O1G B:APC1500 4.6 23.8 1.0
O2G B:APC1500 4.6 20.0 1.0
O2B B:APC1500 4.8 27.9 1.0
O B:HOH2031 4.8 23.2 1.0
CG1 B:ILE1018 4.8 17.0 1.0
CB B:ASP1061 4.8 17.4 1.0
C B:ASP1017 4.9 17.5 1.0
O B:ASP1061 4.9 15.4 1.0
PA B:APC1500 5.0 30.9 1.0
O B:HOH2111 5.0 51.6 1.0
C B:ASP1061 5.0 15.3 1.0
O B:HOH2112 5.0 19.1 1.0
CA B:ASP1017 5.0 19.0 1.0

Reference:

C.Steegborn, T.N.Litvin, L.R.Levin, J.Buck, H.Wu. Bicarbonate Activation of Adenylyl Cyclase Via Promotion of Catalytic Active Site Closure and Metal Recruitment Nat.Struct.Mol.Biol. V. 12 32 2005.
ISSN: ISSN 1545-9993
PubMed: 15619637
DOI: 10.1038/NSMB880
Page generated: Mon Jan 25 16:03:09 2021

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