Atomistry » Chlorine » PDB 5u0i-5u6x » 5u0i
Atomistry »
  Chlorine »
    PDB 5u0i-5u6x »
      5u0i »

Chlorine in PDB 5u0i: C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form

Enzymatic activity of C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form

All present enzymatic activity of C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form:
3.5.1.2;

Protein crystallography data

The structure of C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form, PDB code: 5u0i was solved by C.C.Pasquali, A.Gonzalez, S.M.G.Dias, A.L.B.Ambrosio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.09 / 1.42
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 75.290, 75.290, 88.310, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / 18

Other elements in 5u0i:

The structure of C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form also contains other interesting chemical elements:

Sodium (Na) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form (pdb code 5u0i). 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 C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form, PDB code: 5u0i:

Chlorine binding site 1 out of 1 in 5u0i

Go back to Chlorine Binding Sites List in 5u0i
Chlorine binding site 1 out of 1 in the C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl701

b:32.3
occ:1.00
 NH2 A:ARG582 3.0 24.8 1.0
N A:LYS616 3.1 18.5 1.0
O A:HOH871 3.2 36.5 1.0
CA A:PRO615 3.8 17.4 1.0
CB A:LYS616 3.9 22.3 1.0
CZ A:ARG582 3.9 23.9 1.0
C A:PRO615 3.9 18.3 1.0
CA A:LYS616 4.0 17.6 1.0
O A:LYS616 4.0 17.3 1.0
NH1 A:ARG582 4.0 20.9 1.0
CG A:LYS616 4.4 28.0 1.0
CB A:PRO615 4.5 17.1 1.0
C A:LYS616 4.5 16.5 1.0
O A:PHE614 4.6 22.7 1.0
CE A:LYS616 4.7 48.7 1.0
OD1 A:ASN612 4.8 31.8 1.0
O A:HOH853 4.9 40.2 1.0
N A:PRO615 5.0 18.2 1.0

Reference:

C.C.Pasquali, Z.Islam, D.Adamoski, I.M.Ferreira, R.D.Righeto, J.Bettini, R.V.Portugal, W.W.Yue, A.Gonzalez, S.M.G.Dias, A.L.B.Ambrosio. The Origin and Evolution of Human Glutaminases and Their Atypical C-Terminal Ankyrin Repeats. J. Biol. Chem. V. 292 11572 2017.
ISSN: ESSN 1083-351X
PubMed: 28526749
DOI: 10.1074/JBC.M117.787291
Page generated: Fri Jul 26 17:52:06 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy