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Chlorine in PDB 8up7: Structure of Atypical Asparaginase From Rhodospirillum Rubrum (Mutant K19A)

Enzymatic activity of Structure of Atypical Asparaginase From Rhodospirillum Rubrum (Mutant K19A)

All present enzymatic activity of Structure of Atypical Asparaginase From Rhodospirillum Rubrum (Mutant K19A):
3.5.1.1;

Protein crystallography data

The structure of Structure of Atypical Asparaginase From Rhodospirillum Rubrum (Mutant K19A), PDB code: 8up7 was solved by J.Lubkowski, A.Wlodawer, D.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.11 / 1.70
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 72.106, 77.358, 58.202, 90, 90, 90
R / Rfree (%) 19.9 / 23.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Atypical Asparaginase From Rhodospirillum Rubrum (Mutant K19A) (pdb code 8up7). 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 Structure of Atypical Asparaginase From Rhodospirillum Rubrum (Mutant K19A), PDB code: 8up7:

Chlorine binding site 1 out of 1 in 8up7

Go back to Chlorine Binding Sites List in 8up7
Chlorine binding site 1 out of 1 in the Structure of Atypical Asparaginase From Rhodospirillum Rubrum (Mutant K19A)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Atypical Asparaginase From Rhodospirillum Rubrum (Mutant K19A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl201

b:44.7
occ:0.50
N B:LEU28 3.2 18.2 1.0
CB B:LEU28 3.7 17.5 1.0
CG B:LEU28 3.8 17.5 1.0
CA B:GLY27 4.0 19.1 1.0
CA B:LEU28 4.1 17.9 1.0
C B:GLY27 4.1 17.1 1.0
CD1 B:LEU28 4.2 17.2 1.0
O B:LEU28 4.7 19.4 1.0
C B:LEU28 4.9 18.3 1.0

Reference:

D.Zhang, H.Czapinska, M.Bochtler, A.Wlodawer, J.Lubkowski. Rra, An Enzyme From Rhodospirillum Rubrum, Is A Prototype of A New Family of Short-Chain L-Asparaginases. Protein Sci. V. 33 E4920 2024.
ISSN: ESSN 1469-896X
PubMed: 38501449
DOI: 10.1002/PRO.4920
Page generated: Sun Jul 13 14:58:23 2025

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