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Chlorine in PDB 5xlj: Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432

Protein crystallography data

The structure of Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432, PDB code: 5xlj was solved by S.Y.Cho, W.S.Song, H.J.Hong, S.I.Yoon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.90
Space group P 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 120.386, 120.386, 120.386, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 20.8

Other elements in 5xlj:

The structure of Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432 also contains other interesting chemical elements:

Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432 (pdb code 5xlj). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432, PDB code: 5xlj:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in 5xlj

Go back to Chlorine Binding Sites List in 5xlj
Chlorine binding site 1 out of 5 in the Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432


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 Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:20.4
occ:1.00
NZ A:LYS192 3.0 18.5 1.0
O A:HOH502 3.3 38.9 1.0
CE A:LYS192 3.7 20.9 1.0
O A:HOH433 4.5 16.8 1.0
OD1 A:ASN190 5.0 19.1 1.0

Chlorine binding site 2 out of 5 in 5xlj

Go back to Chlorine Binding Sites List in 5xlj
Chlorine binding site 2 out of 5 in the Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432


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 Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:25.8
occ:1.00
O A:HOH451 3.1 32.4 1.0
N A:GLY165 3.1 11.6 1.0
O A:HOH526 3.2 23.2 1.0
C A:LYS163 3.5 13.7 1.0
CA A:GLY165 3.6 11.9 1.0
CA A:LYS163 3.7 14.4 1.0
O A:LYS163 3.7 13.4 1.0
N A:ALA164 3.8 12.7 1.0
CB A:LYS163 4.0 16.1 1.0
OG A:SER185 4.0 19.7 1.0
C A:ALA164 4.3 11.9 1.0
C A:GLY165 4.4 11.2 1.0
N A:VAL166 4.5 11.2 1.0
CB A:SER185 4.5 14.7 1.0
O A:HOH538 4.6 39.9 1.0
O A:HOH415 4.6 17.3 1.0
CA A:ALA164 4.6 12.3 1.0
CG A:LYS163 4.7 20.4 1.0
O A:VAL166 4.7 11.8 1.0
O A:HOH442 4.9 30.7 1.0
NA A:NA306 4.9 19.9 1.0

Chlorine binding site 3 out of 5 in 5xlj

Go back to Chlorine Binding Sites List in 5xlj
Chlorine binding site 3 out of 5 in the Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:28.6
occ:0.50
NE2 A:GLN221 3.2 14.9 1.0
O A:HOH541 3.6 42.4 1.0
O A:HOH413 3.7 31.5 1.0
CB A:ALA224 4.0 14.8 1.0
CD A:GLN221 4.2 14.2 1.0
OE1 A:GLN221 4.4 14.1 1.0
CA A:ALA224 4.8 13.2 1.0

Chlorine binding site 4 out of 5 in 5xlj

Go back to Chlorine Binding Sites List in 5xlj
Chlorine binding site 4 out of 5 in the Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl304

b:28.7
occ:1.00
N A:LEU101 3.3 17.8 1.0
NE2 A:GLN226 3.4 19.2 1.0
CE A:LYS258 3.5 36.8 1.0
CA A:LYS100 3.9 20.4 1.0
CB A:LEU101 4.1 19.3 1.0
C A:LYS100 4.1 18.2 1.0
O A:LEU101 4.2 17.6 1.0
CA A:LEU101 4.2 17.4 1.0
CG A:LEU101 4.4 22.6 1.0
CG A:LYS258 4.5 31.2 1.0
NZ A:LYS258 4.5 40.5 1.0
CB A:LYS100 4.5 20.4 1.0
CD A:LYS258 4.5 35.0 1.0
CD A:GLN226 4.6 24.2 1.0
CG A:LYS100 4.7 25.9 1.0
C A:LEU101 4.7 17.1 1.0
OE1 A:GLN103 4.7 24.4 1.0
CD1 A:LEU101 4.9 26.5 1.0
O A:ASN99 4.9 24.7 1.0

Chlorine binding site 5 out of 5 in 5xlj

Go back to Chlorine Binding Sites List in 5xlj
Chlorine binding site 5 out of 5 in the Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of the Flagellar Cap Protein Flid D2-D3 Domains From Serratia Marcescens in Space Group P432 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl305

b:31.2
occ:1.00
O A:HOH410 3.0 27.2 1.0
N A:ILE170 3.2 16.0 1.0
NH1 A:ARG156 3.3 22.7 1.0
CD A:ARG156 3.6 18.7 1.0
CA A:SER169 3.7 15.3 1.0
CB A:SER169 4.0 16.5 1.0
C A:SER169 4.0 15.6 1.0
CZ A:ARG156 4.1 23.6 1.0
CB A:ILE170 4.2 17.9 1.0
CA A:ILE170 4.2 16.5 1.0
O A:ILE170 4.2 17.5 1.0
NE A:ARG156 4.2 19.1 1.0
CG1 A:ILE170 4.6 18.9 1.0
C A:ILE170 4.7 16.8 1.0
CG A:ARG156 4.8 14.6 1.0
O A:HOH535 4.9 32.6 1.0
O A:ALA168 4.9 13.4 1.0

Reference:

S.Y.Cho, W.S.Song, H.J.Hong, G.S.Lee, S.G.Kang, H.J.Ko, P.H.Kim, S.I.Yoon. Tetrameric Structure of the Flagellar Cap Protein Flid From Serratia Marcescens. Biochem. Biophys. Res. V. 489 63 2017COMMUN..
ISSN: ESSN 1090-2104
PubMed: 28527888
DOI: 10.1016/J.BBRC.2017.05.093
Page generated: Sat Jul 12 10:41:17 2025

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