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Chlorine in PDB 4clk: 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: 4clk 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) 86.82 / 2.20
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 100.250, 100.250, 97.450, 90.00, 90.00, 120.00
R / Rfree (%) 17.605 / 23.664

Other elements in 4clk:

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

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate (pdb code 4clk). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with Alpha,Beta-Methyleneadenosine-5'-Triphosphate, PDB code: 4clk:

Chlorine binding site 1 out of 1 in 4clk

Go back to Chlorine Binding Sites List in 4clk
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl1469

b:26.7
occ:1.00
 NZ A:LYS95 2.8 23.7 1.0
O A:HOH2082 3.2 34.4 1.0
N A:VAL167 3.3 25.5 1.0
CE A:LYS95 3.6 25.2 1.0
O A:HOH2066 3.7 39.1 1.0
CG2 A:VAL167 3.7 24.3 1.0
CA A:LEU166 3.8 25.9 1.0
CD A:LYS95 3.8 27.2 1.0
C A:LEU166 4.0 25.2 1.0
CD2 A:LEU166 4.1 37.3 1.0
CD2 A:LEU102 4.3 23.8 1.0
CA A:VAL167 4.4 26.4 1.0
O A:VAL335 4.5 34.6 1.0
O A:VAL167 4.5 27.8 1.0
O A:PHE165 4.6 24.9 1.0
CB A:VAL167 4.6 25.4 1.0
CB A:PHE336 4.6 38.8 1.0
CE2 A:PHE165 4.7 22.8 1.0
O A:HOH2144 4.7 39.6 1.0
CA A:PHE336 4.7 36.5 1.0
CB A:LEU166 4.8 30.5 1.0
N A:LEU166 4.8 23.4 1.0
CB A:LYS95 4.8 23.6 1.0
CG A:LYS95 5.0 26.5 1.0
C A:VAL167 5.0 27.3 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: Sun Jul 21 11:20:29 2024

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