Chlorine in PDB 5xct: Crystal Structure of P20.1 Fv-Clasp Fragment with Its Antigen Peptide

Protein crystallography data

The structure of Crystal Structure of P20.1 Fv-Clasp Fragment with Its Antigen Peptide, PDB code: 5xct was solved by T.Arimori, J.Takagi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.58 / 1.17
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.100, 55.159, 62.484, 90.00, 93.16, 90.00
R / Rfree (%) 15.2 / 18.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of P20.1 Fv-Clasp Fragment with Its Antigen Peptide (pdb code 5xct). 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 P20.1 Fv-Clasp Fragment with Its Antigen Peptide, PDB code: 5xct:

Chlorine binding site 1 out of 1 in 5xct

Go back to Chlorine Binding Sites List in 5xct
Chlorine binding site 1 out of 1 in the Crystal Structure of P20.1 Fv-Clasp Fragment with Its Antigen Peptide


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 P20.1 Fv-Clasp Fragment with Its Antigen Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl201

b:52.9
occ:1.00
O A:HOH502 2.6 43.1 1.0
O A:HOH365 2.8 25.4 1.0
O A:HOH464 2.8 25.4 1.0
CG A:LYS130 3.7 19.6 1.0
CA A:LYS130 3.9 13.0 1.0
CB A:LYS130 4.0 14.9 1.0
CD1 A:LEU133 4.1 31.4 1.0
O A:HOH490 4.5 30.1 0.9
CD A:LYS130 4.5 26.4 1.0
O A:LYS130 4.5 14.9 1.0
CB A:LEU133 4.6 24.0 1.0
O A:HOH368 4.7 14.9 0.9
C A:LYS130 4.7 12.3 1.0
N A:LYS130 4.9 12.4 1.0
O A:HOH503 4.9 50.4 0.9
CG A:LEU133 5.0 29.5 1.0

Reference:

T.Arimori, Y.Kitago, M.Umitsu, Y.Fujii, R.Asaki, K.Tamura-Kawakami, J.Takagi. Fv-Clasp: An Artificially Designed Small Antibody Fragment with Improved Production Compatibility, Stability, and Crystallizability Structure V. 25 1611 2017.
ISSN: ISSN 1878-4186
PubMed: 28919443
DOI: 10.1016/J.STR.2017.08.011
Page generated: Sat Dec 12 12:38:42 2020

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