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Chlorine in PDB 4dy5: Crystal Structure of Salmonella Typhimurium Plig, A Periplasmic Lysozyme Inhibitor of G-Type Lysozyme

Protein crystallography data

The structure of Crystal Structure of Salmonella Typhimurium Plig, A Periplasmic Lysozyme Inhibitor of G-Type Lysozyme, PDB code: 4dy5 was solved by S.Leysen, V.Theuwis, L.Vanderkelen, C.W.Michiels, S.V.Strelkov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.60 / 1.78
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.338, 89.199, 97.637, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 21.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Salmonella Typhimurium Plig, A Periplasmic Lysozyme Inhibitor of G-Type Lysozyme (pdb code 4dy5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Salmonella Typhimurium Plig, A Periplasmic Lysozyme Inhibitor of G-Type Lysozyme, PDB code: 4dy5:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 4dy5

Go back to Chlorine Binding Sites List in 4dy5
Chlorine binding site 1 out of 3 in the Crystal Structure of Salmonella Typhimurium Plig, A Periplasmic Lysozyme Inhibitor of G-Type Lysozyme


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 Salmonella Typhimurium Plig, A Periplasmic Lysozyme Inhibitor of G-Type Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl201

b:80.1
occ:1.00
O A:HOH418 2.5 49.6 1.0
OG A:SER65 3.0 30.3 1.0
O A:HOH395 3.2 56.0 1.0
CB A:SER65 3.8 25.4 1.0
C A:SER65 3.9 21.7 1.0
N A:ILE66 3.9 18.4 1.0
O A:SER65 4.0 19.3 1.0
C A:ILE66 4.0 22.0 1.0
O A:SER127 4.0 23.9 0.6
N A:SER67 4.1 18.2 1.0
O A:SER127 4.1 23.5 0.4
CA A:ILE66 4.1 17.6 1.0
NH1 A:ARG39 4.2 62.3 1.0
O A:ILE66 4.4 19.3 1.0
CA A:SER67 4.5 20.5 1.0
CA A:SER65 4.5 19.2 1.0
N A:ASN129 4.6 25.8 1.0
CB A:ASN129 4.6 28.0 1.0
CB A:SER67 4.6 25.3 1.0
C A:SER127 4.8 22.8 0.6
C A:SER127 4.8 22.2 0.4
OG A:SER127 4.8 28.1 0.6

Chlorine binding site 2 out of 3 in 4dy5

Go back to Chlorine Binding Sites List in 4dy5
Chlorine binding site 2 out of 3 in the Crystal Structure of Salmonella Typhimurium Plig, A Periplasmic Lysozyme Inhibitor of G-Type Lysozyme


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 Salmonella Typhimurium Plig, A Periplasmic Lysozyme Inhibitor of G-Type Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl201

b:80.6
occ:1.00
NE2 B:GLN131 3.6 43.9 1.0
CD B:GLN98 3.9 28.0 1.0
NE2 B:GLN98 3.9 27.5 1.0
O B:ASN96 4.0 25.7 1.0
CG B:GLN98 4.1 24.2 1.0
OE1 B:GLN98 4.2 29.9 1.0
O B:HOH359 4.4 41.0 1.0
OE1 B:GLN131 4.5 58.0 1.0
CD B:GLN131 4.5 50.9 1.0
CG B:HIS63 4.7 26.3 1.0
CB B:HIS63 4.7 23.4 1.0
O B:HOH325 4.9 24.7 1.0
CB B:ASN96 4.9 26.9 1.0
ND1 B:HIS63 5.0 35.7 1.0

Chlorine binding site 3 out of 3 in 4dy5

Go back to Chlorine Binding Sites List in 4dy5
Chlorine binding site 3 out of 3 in the Crystal Structure of Salmonella Typhimurium Plig, A Periplasmic Lysozyme Inhibitor of G-Type Lysozyme


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 Salmonella Typhimurium Plig, A Periplasmic Lysozyme Inhibitor of G-Type Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl201

b:64.9
occ:1.00
O C:HOH392 2.3 50.2 1.0
NZ C:LYS110 3.4 25.8 1.0
ND2 C:ASN26 3.5 60.7 1.0
CB B:SER41 3.9 30.9 1.0
OG B:SER41 3.9 46.8 1.0
OH C:TYR49 3.9 32.9 1.0
OG1 C:THR51 4.3 22.0 1.0
CE1 C:TYR49 4.3 25.6 1.0
O C:HOH315 4.4 31.1 1.0
CE C:LYS110 4.6 30.6 1.0
OE1 C:GLU108 4.6 40.7 1.0
CZ C:TYR49 4.6 32.4 1.0
CG C:ASN26 4.7 51.7 1.0

Reference:

S.Leysen, L.Vanderkelen, K.Van Asten, S.Vanheuverzwijn, V.Theuwis, C.W.Michiels, S.V.Strelkov. Structural Characterization of the Plig Lysozyme Inhibitor Family. J.Struct.Biol. V. 180 235 2012.
ISSN: ISSN 1047-8477
PubMed: 22634186
DOI: 10.1016/J.JSB.2012.05.006
Page generated: Fri Jul 11 14:33:21 2025

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