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Chlorine in PDB 3ago: Crystal Structure of Ustilago Sphaerogena Ribonuclease U2 Complexed with Adenosine 3'-Monophosphate

Enzymatic activity of Crystal Structure of Ustilago Sphaerogena Ribonuclease U2 Complexed with Adenosine 3'-Monophosphate

All present enzymatic activity of Crystal Structure of Ustilago Sphaerogena Ribonuclease U2 Complexed with Adenosine 3'-Monophosphate:
3.1.27.4;

Protein crystallography data

The structure of Crystal Structure of Ustilago Sphaerogena Ribonuclease U2 Complexed with Adenosine 3'-Monophosphate, PDB code: 3ago was solved by S.Noguchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.71 / 0.99
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 34.586, 39.425, 31.646, 90.00, 108.98, 90.00
R / Rfree (%) 15 / 16.2

Other elements in 3ago:

The structure of Crystal Structure of Ustilago Sphaerogena Ribonuclease U2 Complexed with Adenosine 3'-Monophosphate also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Ustilago Sphaerogena Ribonuclease U2 Complexed with Adenosine 3'-Monophosphate (pdb code 3ago). 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 Ustilago Sphaerogena Ribonuclease U2 Complexed with Adenosine 3'-Monophosphate, PDB code: 3ago:

Chlorine binding site 1 out of 1 in 3ago

Go back to Chlorine Binding Sites List in 3ago
Chlorine binding site 1 out of 1 in the Crystal Structure of Ustilago Sphaerogena Ribonuclease U2 Complexed with Adenosine 3'-Monophosphate


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 Ustilago Sphaerogena Ribonuclease U2 Complexed with Adenosine 3'-Monophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl118

b:10.1
occ:1.00
NE A:ARG35 2.8 16.7 0.5
OH A:TYR71 3.1 10.6 1.0
OG A:SER73 3.2 8.5 1.0
CD A:ARG35 3.3 17.5 0.5
ND2 A:ASN38 3.3 15.9 1.0
N A:TYR39 3.6 8.2 1.0
CA A:ASN38 3.7 11.5 1.0
CB A:ALA31 3.8 8.4 1.0
CD2 A:TYR39 3.8 7.7 1.0
CE1 A:TYR71 3.8 7.2 1.0
CB A:ASN38 3.9 12.8 1.0
CZ A:ARG35 3.9 15.2 0.5
CB A:SER73 3.9 8.0 1.0
CZ A:TYR71 3.9 7.7 1.0
CG A:ARG35 4.0 18.0 0.5
CG A:ASN38 4.1 13.9 1.0
CE2 A:TYR78 4.2 17.1 1.0
NH2 A:ARG35 4.2 15.0 0.5
C A:ASN38 4.2 10.3 1.0
CD2 A:TYR78 4.3 13.8 1.0
CD A:ARG35 4.5 15.6 0.5
CE2 A:TYR39 4.5 7.3 1.0
CB A:ARG35 4.5 18.2 0.5
CB A:ARG35 4.6 18.1 0.5
CA A:ALA31 4.6 6.8 1.0
CB A:TYR39 4.7 8.7 1.0
CG A:TYR39 4.7 7.8 1.0
O A:HOH178 4.7 20.5 1.0
C A:ALA31 4.7 8.0 1.0
CA A:TYR39 4.7 8.2 1.0
N A:ASN38 4.9 13.1 1.0
CG A:ARG35 4.9 17.0 0.5
O A:ALA31 4.9 9.2 1.0
N A:GLY33 5.0 10.3 1.0

Reference:

S.Noguchi, S.Noguchi. N/A N/A.
ISSN: ISSN 0907-4449
PubMed: 20606265
DOI: 10.1107/S0907444910019621
Page generated: Sat Dec 12 09:31:22 2020

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