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Chlorine in PDB 4ust: Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium

Enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium

All present enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium:
4.6.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium, PDB code: 4ust 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) 86.90 / 1.90
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 100.340, 100.340, 97.420, 90.00, 90.00, 120.00
R / Rfree (%) 16.091 / 20.248

Other elements in 4ust:

The structure of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium (pdb code 4ust). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium, PDB code: 4ust:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 4ust

Go back to Chlorine Binding Sites List in 4ust
Chlorine binding site 1 out of 2 in the Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium


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 with Pyrophosphate Resulting From Soaking with Gtp and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1469

b:28.5
occ:1.00
 NZ A:LYS95 3.0 25.7 1.0
O A:HOH2110 3.1 30.4 1.0
N A:VAL167 3.4 24.9 1.0
CE A:LYS95 3.7 27.9 1.0
CA A:LEU166 3.8 25.8 1.0
CG2 A:VAL167 3.8 25.4 1.0
CD A:LYS95 4.0 30.0 1.0
C A:LEU166 4.1 25.8 1.0
O A:ACT1472 4.1 60.2 1.0
CD2 A:LEU166 4.1 49.0 1.0
CD2 A:LEU102 4.3 26.2 1.0
CB A:PHE336 4.4 42.4 1.0
CA A:VAL167 4.5 26.4 1.0
O A:HOH2117 4.5 40.8 1.0
O A:PHE165 4.6 23.0 1.0
CB A:LEU166 4.6 34.9 1.0
O A:VAL335 4.6 35.0 1.0
CB A:VAL167 4.6 25.1 1.0
CA A:PHE336 4.6 37.1 1.0
O A:VAL167 4.7 26.8 1.0
CE2 A:PHE165 4.7 25.7 1.0
N A:LEU166 4.8 23.2 1.0
CB A:LYS95 4.9 24.6 1.0

Chlorine binding site 2 out of 2 in 4ust

Go back to Chlorine Binding Sites List in 4ust
Chlorine binding site 2 out of 2 in the Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Gtp and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1470

b:41.6
occ:1.00
 N A:VAL335 3.1 26.0 1.0
O A:HOH2109 3.1 23.5 1.0
CE A:LYS95 3.4 27.9 1.0
NZ A:LYS95 3.4 25.7 1.0
O A:VAL335 3.5 35.0 1.0
CA A:LYS334 3.7 29.0 1.0
O A:HOH2106 3.7 44.9 1.0
CD A:LYS334 3.8 33.0 1.0
C A:LYS334 3.8 31.3 1.0
CD A:LYS95 3.9 30.0 1.0
O A:HOH2009 4.0 59.6 1.0
CA A:VAL335 4.0 28.6 1.0
CG A:LYS334 4.1 38.4 1.0
C A:VAL335 4.2 33.4 1.0
CB A:VAL335 4.2 29.9 1.0
O A:PHE165 4.3 23.0 1.0
CG2 A:VAL335 4.4 32.2 1.0
O A:HOH2008 4.4 41.2 1.0
CB A:LYS334 4.4 33.7 1.0
ND1 A:HIS164 4.5 26.9 1.0
O A:ASN333 4.7 30.2 1.0
N A:LYS334 4.7 26.4 1.0
CG A:LYS95 4.8 29.9 1.0
O A:HOH2104 4.8 35.3 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: Fri Jul 26 02:28:00 2024

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