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: Sat Dec 12 12:29:52 2020

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