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Chlorine in PDB 5lbd: Crystal Structure of the N-Domain of HMA6, A Copper-Transporting P- Type Atpase

Enzymatic activity of Crystal Structure of the N-Domain of HMA6, A Copper-Transporting P- Type Atpase

All present enzymatic activity of Crystal Structure of the N-Domain of HMA6, A Copper-Transporting P- Type Atpase:
3.6.3.54;

Protein crystallography data

The structure of Crystal Structure of the N-Domain of HMA6, A Copper-Transporting P- Type Atpase, PDB code: 5lbd was solved by H.Mayerhofer, S.Ravaud, E.Pebay-Peyroula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.96 / 1.50
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.800, 65.191, 85.590, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 20.7

Other elements in 5lbd:

The structure of Crystal Structure of the N-Domain of HMA6, A Copper-Transporting P- Type Atpase also contains other interesting chemical elements:

Iodine (I) 5 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the N-Domain of HMA6, A Copper-Transporting P- Type Atpase (pdb code 5lbd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the N-Domain of HMA6, A Copper-Transporting P- Type Atpase, PDB code: 5lbd:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5lbd

Go back to Chlorine Binding Sites List in 5lbd
Chlorine binding site 1 out of 2 in the Crystal Structure of the N-Domain of HMA6, A Copper-Transporting P- Type Atpase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the N-Domain of HMA6, A Copper-Transporting P- Type Atpase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl802

b:25.5
occ:1.00
H B:GLU693 3.0 27.6 1.0
N B:NH4806 3.2 25.4 1.0
HB2 B:GLU693 3.2 32.2 1.0
HB B:THR691 3.3 30.9 1.0
HB3 B:LEU692 3.4 41.3 1.0
H B:LEU692 3.7 26.2 1.0
N B:GLU693 3.8 23.0 1.0
HB3 B:GLU693 3.9 32.2 1.0
CB B:GLU693 3.9 26.8 1.0
N B:LEU692 4.2 21.9 1.0
CB B:THR691 4.2 25.8 1.0
CB B:LEU692 4.4 34.4 1.0
HG1 B:THR691 4.4 27.0 1.0
CA B:GLU693 4.5 26.5 1.0
OG1 B:THR691 4.6 22.5 1.0
CA B:LEU692 4.6 26.6 1.0
C B:LEU692 4.7 26.2 1.0
HB2 B:LEU692 4.8 41.3 1.0
HG21 B:THR691 4.8 28.4 1.0
HD23 B:LEU692 4.9 49.6 1.0
HA B:GLU693 4.9 31.8 1.0
C B:THR691 5.0 18.8 1.0
CG2 B:THR691 5.0 23.6 1.0

Chlorine binding site 2 out of 2 in 5lbd

Go back to Chlorine Binding Sites List in 5lbd
Chlorine binding site 2 out of 2 in the Crystal Structure of the N-Domain of HMA6, A Copper-Transporting P- Type Atpase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the N-Domain of HMA6, A Copper-Transporting P- Type Atpase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl804

b:48.1
occ:1.00
HA2 B:GLY690 3.2 20.9 1.0
O B:SER676 3.5 23.4 1.0
HA2 B:GLY677 3.6 21.6 1.0
HG23 B:THR691 3.8 28.4 1.0
HG12 B:VAL719 3.9 48.2 1.0
HA3 B:GLY690 3.9 20.9 1.0
CA B:GLY690 4.0 17.4 1.0
C B:SER676 4.0 24.1 1.0
HE2 B:HIS645 4.0 59.9 1.0
H B:THR691 4.1 22.1 1.0
CA B:GLY677 4.3 18.0 1.0
N B:THR691 4.4 18.4 1.0
N B:GLY677 4.4 19.2 1.0
HD2 B:HIS645 4.4 62.0 1.0
C B:GLY690 4.4 19.1 1.0
HG22 B:THR691 4.5 28.4 1.0
O B:HOH922 4.5 39.9 1.0
O B:HOH910 4.6 37.9 1.0
CG2 B:THR691 4.6 23.6 1.0
HG11 B:VAL719 4.6 48.2 1.0
HA3 B:GLY677 4.6 21.6 1.0
NE2 B:HIS645 4.7 49.9 1.0
CG1 B:VAL719 4.7 40.2 1.0
N B:SER676 4.7 23.6 1.0
CA B:SER676 4.7 19.5 1.0
HA B:SER676 4.8 23.4 1.0
C B:GLY675 4.8 33.3 1.0
CD2 B:HIS645 4.9 51.7 1.0
O B:HOH907 4.9 35.8 1.0
H B:SER676 4.9 28.4 1.0
O B:GLY675 5.0 34.8 1.0
H B:GLY677 5.0 23.1 1.0

Reference:

H.Mayerhofer, E.Sautron, N.Rolland, P.Catty, D.Seigneurin-Berny, E.Pebay-Peyroula, S.Ravaud. Structural Insights Into the Nucleotide-Binding Domains of the P1B-Type Atpases HMA6 and HMA8 From Arabidopsis Thaliana. Plos One V. 11 65666 2016.
ISSN: ESSN 1932-6203
PubMed: 27802305
DOI: 10.1371/JOURNAL.PONE.0165666
Page generated: Sat Dec 12 12:01:36 2020

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