Atomistry » Chlorine » PDB 4oz2-4p8p » 4p2x
Atomistry »
  Chlorine »
    PDB 4oz2-4p8p »
      4p2x »

Chlorine in PDB 4p2x: Swapped Dimer of Mycobacterial Adenylyl Cyclase RV1625C: Form 2

Enzymatic activity of Swapped Dimer of Mycobacterial Adenylyl Cyclase RV1625C: Form 2

All present enzymatic activity of Swapped Dimer of Mycobacterial Adenylyl Cyclase RV1625C: Form 2:
4.6.1.1;

Protein crystallography data

The structure of Swapped Dimer of Mycobacterial Adenylyl Cyclase RV1625C: Form 2, PDB code: 4p2x was solved by D.V.Barathy, R.Mattoo, S.S.Visweswariah, K.Suguna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.76 / 2.40
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 75.570, 75.570, 133.170, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 26

Other elements in 4p2x:

The structure of Swapped Dimer of Mycobacterial Adenylyl Cyclase RV1625C: Form 2 also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Swapped Dimer of Mycobacterial Adenylyl Cyclase RV1625C: Form 2 (pdb code 4p2x). 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 Swapped Dimer of Mycobacterial Adenylyl Cyclase RV1625C: Form 2, PDB code: 4p2x:

Chlorine binding site 1 out of 1 in 4p2x

Go back to Chlorine Binding Sites List in 4p2x
Chlorine binding site 1 out of 1 in the Swapped Dimer of Mycobacterial Adenylyl Cyclase RV1625C: Form 2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Swapped Dimer of Mycobacterial Adenylyl Cyclase RV1625C: Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl503

b:47.5
occ:1.00
NE2 B:GLN317 2.5 49.7 1.0
NH1 A:ARG395 2.7 52.7 1.0
CD B:GLN317 3.0 47.1 1.0
N B:THR316 3.2 28.4 1.0
OE1 B:GLN317 3.2 53.7 1.0
CB B:THR316 3.4 29.6 1.0
N B:GLN317 3.5 32.6 1.0
OG1 B:THR316 3.6 27.8 1.0
C B:ASP314 3.6 30.4 1.0
CA B:THR316 3.7 29.6 1.0
CA B:ASP314 3.7 31.1 1.0
O B:PRO313 3.7 25.8 1.0
N B:HIS315 3.7 28.8 1.0
CZ A:ARG395 4.0 50.6 1.0
C B:THR316 4.1 31.1 1.0
O B:ASP314 4.1 31.6 1.0
C B:HIS315 4.2 29.1 1.0
CG B:GLN317 4.2 41.6 1.0
CB B:GLN317 4.5 38.1 1.0
C B:PRO313 4.5 26.9 1.0
CD A:ARG395 4.5 43.2 1.0
CA B:HIS315 4.5 28.4 1.0
N B:ASP314 4.6 28.9 1.0
CA B:GLN317 4.6 34.7 1.0
CB A:ARG395 4.6 41.2 1.0
NE A:ARG395 4.7 46.7 1.0
CG2 B:THR316 4.7 30.2 1.0
CB B:ASP314 4.7 31.9 1.0
CD2 B:HIS315 4.8 27.6 1.0
NH2 A:ARG395 4.8 53.2 1.0
CG B:HIS315 4.9 27.4 1.0
NE2 B:HIS315 4.9 28.4 1.0
O A:ARG395 4.9 42.8 1.0
CG A:ARG395 5.0 42.0 1.0

Reference:

D.Barathy, R.Mattoo, S.Visweswariah, K.Suguna. New Structural Forms of A Mycobacterial Adenylyl Cyclase RV1625C. Iucrj V. 1 338 2014.
ISSN: ESSN 2052-2525
PubMed: 25295175
DOI: 10.1107/S2052252514016741
Page generated: Thu Jul 25 23:46:57 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy