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Sodium in PDB 5teq: C20S C293G Mutant N-Terminal Human Atp Citrate Lyase Bound to Citrate

Enzymatic activity of C20S C293G Mutant N-Terminal Human Atp Citrate Lyase Bound to Citrate

All present enzymatic activity of C20S C293G Mutant N-Terminal Human Atp Citrate Lyase Bound to Citrate:
2.3.3.8;

Protein crystallography data

The structure of C20S C293G Mutant N-Terminal Human Atp Citrate Lyase Bound to Citrate, PDB code: 5teq was solved by J.Hu, M.E.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.46 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 95.110, 73.100, 131.120, 90.00, 97.89, 90.00
R / Rfree (%) 20.2 / 24.6

Sodium Binding Sites:

The binding sites of Sodium atom in the C20S C293G Mutant N-Terminal Human Atp Citrate Lyase Bound to Citrate (pdb code 5teq). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the C20S C293G Mutant N-Terminal Human Atp Citrate Lyase Bound to Citrate, PDB code: 5teq:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 5teq

Go back to Sodium Binding Sites List in 5teq
Sodium binding site 1 out of 2 in the C20S C293G Mutant N-Terminal Human Atp Citrate Lyase Bound to Citrate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of C20S C293G Mutant N-Terminal Human Atp Citrate Lyase Bound to Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na903

b:45.3
occ:1.00
O A:ASP257 2.4 39.8 1.0
OD1 A:ASP257 2.4 35.0 1.0
O A:ALA262 2.5 29.0 1.0
O A:SER260 2.6 44.5 1.0
O A:HOH1216 2.9 39.4 1.0
CG A:ASP257 3.2 35.0 1.0
HA A:SER263 3.3 42.0 1.0
C A:ASP257 3.3 36.2 1.0
HA A:ASP257 3.3 46.5 1.0
C A:ALA262 3.6 31.4 1.0
C A:SER260 3.7 46.5 1.0
CA A:ASP257 3.7 38.8 1.0
OD2 A:ASP257 3.9 39.1 1.0
OG A:SER260 3.9 41.9 0.5
HG A:SER260 4.0 50.2 0.5
CB A:ASP257 4.1 31.6 1.0
H A:SER260 4.1 59.9 0.5
H A:SER260 4.1 59.9 0.5
HB3 A:SER260 4.1 53.3 0.5
CA A:SER263 4.1 35.0 1.0
C A:GLY261 4.2 45.4 1.0
O A:GLY261 4.2 43.9 1.0
HA2 A:GLY261 4.2 55.1 1.0
H A:LEU264 4.3 39.0 1.0
N A:SER263 4.3 38.0 1.0
N A:ALA262 4.5 37.8 1.0
HA A:ALA258 4.5 53.0 1.0
N A:ALA258 4.5 37.6 1.0
CA A:GLY261 4.6 45.9 1.0
HB3 A:ASP257 4.6 37.9 1.0
N A:GLY261 4.6 44.6 1.0
CA A:SER260 4.6 41.3 0.5
CA A:SER260 4.6 41.2 0.5
CA A:ALA262 4.7 35.4 1.0
N A:SER260 4.7 49.9 1.0
HB2 A:ASP257 4.8 37.9 1.0
CB A:SER260 4.8 44.4 0.5
CB A:SER260 4.8 45.2 0.5
N A:LEU264 4.8 32.5 1.0
H A:ALA262 4.9 45.3 1.0
CA A:ALA258 4.9 44.1 1.0
HB2 A:SER263 5.0 28.7 1.0
C A:SER263 5.0 29.2 1.0
HB2 A:SER260 5.0 54.2 0.5

Sodium binding site 2 out of 2 in 5teq

Go back to Sodium Binding Sites List in 5teq
Sodium binding site 2 out of 2 in the C20S C293G Mutant N-Terminal Human Atp Citrate Lyase Bound to Citrate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of C20S C293G Mutant N-Terminal Human Atp Citrate Lyase Bound to Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na903

b:51.0
occ:1.00
O B:ASP257 2.4 42.9 1.0
O B:SER260 2.5 49.0 1.0
OD1 B:ASP257 2.6 34.2 1.0
O B:ALA262 2.7 36.2 1.0
CG B:ASP257 3.4 37.2 1.0
C B:ASP257 3.4 40.2 1.0
HA B:SER263 3.5 47.6 1.0
HA B:ASP257 3.6 46.1 1.0
C B:SER260 3.6 43.0 1.0
HG B:SER260 3.8 50.3 0.5
C B:ALA262 3.8 34.9 1.0
OG B:SER260 3.8 41.9 0.5
H B:SER260 3.9 59.4 0.5
H B:SER260 3.9 59.4 0.5
CA B:ASP257 3.9 38.5 1.0
OD2 B:ASP257 4.0 42.1 1.0
HA2 B:GLY261 4.0 53.0 1.0
HB3 B:SER260 4.1 61.7 0.5
C B:GLY261 4.1 43.9 1.0
O B:GLY261 4.2 40.8 1.0
CB B:ASP257 4.3 36.2 1.0
O B:HOH1227 4.3 43.4 1.0
CA B:SER263 4.4 39.6 1.0
HA B:ALA258 4.4 58.0 1.0
CA B:GLY261 4.4 44.1 1.0
N B:GLY261 4.4 38.7 1.0
N B:ALA262 4.5 37.6 1.0
CA B:SER260 4.5 42.3 0.5
CA B:SER260 4.5 42.1 0.5
N B:SER263 4.5 39.9 1.0
N B:ALA258 4.5 37.9 1.0
H B:LEU264 4.5 42.8 1.0
N B:SER260 4.6 49.5 1.0
CB B:SER260 4.7 49.6 0.5
CB B:SER260 4.7 51.5 0.5
HB3 B:ASP257 4.7 43.4 1.0
CA B:ALA262 4.8 33.1 1.0
CA B:ALA258 4.9 48.3 1.0
H B:ALA262 4.9 45.1 1.0
HB2 B:ASP257 5.0 43.4 1.0

Reference:

J.Hu, A.Komakula, M.E.Fraser. Binding of Hydroxycitrate to Human Atp-Citrate Lyase. Acta Crystallogr D Struct V. 73 660 2017BIOL.
ISSN: ISSN 2059-7983
PubMed: 28777081
DOI: 10.1107/S2059798317009871
Page generated: Tue Oct 8 00:08:50 2024

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