Chlorine in PDB 6gus: Crystal Structure of Protein E From Non-Typeable Haemophilus Influenzae

Protein crystallography data

The structure of Crystal Structure of Protein E From Non-Typeable Haemophilus Influenzae, PDB code: 6gus was solved by D.Somers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.92
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 77.670, 77.670, 66.130, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 24.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Protein E From Non-Typeable Haemophilus Influenzae (pdb code 6gus). 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 Crystal Structure of Protein E From Non-Typeable Haemophilus Influenzae, PDB code: 6gus:

Chlorine binding site 1 out of 1 in 6gus

Go back to Chlorine Binding Sites List in 6gus
Chlorine binding site 1 out of 1 in the Crystal Structure of Protein E From Non-Typeable Haemophilus Influenzae


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 Protein E From Non-Typeable Haemophilus Influenzae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl204

b:69.4
occ:1.00
OG A:SER38 3.2 42.4 0.5
N A:SER38 3.4 37.7 0.5
N A:SER38 3.4 38.9 0.5
O A:HOH358 3.8 64.7 1.0
CB A:SER38 3.9 45.0 0.5
CB A:SER38 3.9 51.2 0.5
CA A:ARG37 4.0 38.6 1.0
CG A:ARG37 4.1 39.4 1.0
C A:ARG37 4.2 37.7 1.0
CA A:SER38 4.2 40.2 0.5
CA A:SER38 4.2 43.3 0.5
CB A:ARG37 4.5 38.5 1.0
O A:VAL36 4.8 47.7 1.0

Reference:

N.Blais, D.Somers, D.Faubert, S.Labbe, C.Castado, C.Ysebaert, L.P.Gagnon, J.Champagne, M.Gagne, D.Martin. Design and Characterization of Protein E-Pila, A Candidate Fusion Antigen For Nontypeable Haemophilus Influenzae Vaccine. Infect.Immun. V. 87 2019.
ISSN: ESSN 1098-5522
PubMed: 31085711
DOI: 10.1128/IAI.00022-19
Page generated: Sat Dec 12 13:02:50 2020

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