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Chlorine in PDB 3bz5: Functional Domain of Inlj From Listeria Monocytogenes Includes A Cysteine Ladder

Protein crystallography data

The structure of Functional Domain of Inlj From Listeria Monocytogenes Includes A Cysteine Ladder, PDB code: 3bz5 was solved by M.Bublitz, C.Holland, C.Sabet, J.Reichelt, P.Cossart, D.W.Heinz, H.Bierne, W.D.Schubert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.28 / 2.70
Space group I 2 3
Cell size a, b, c (Å), α, β, γ (°) 159.272, 159.272, 159.272, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 25.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Functional Domain of Inlj From Listeria Monocytogenes Includes A Cysteine Ladder (pdb code 3bz5). 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 Functional Domain of Inlj From Listeria Monocytogenes Includes A Cysteine Ladder, PDB code: 3bz5:

Chlorine binding site 1 out of 1 in 3bz5

Go back to Chlorine Binding Sites List in 3bz5
Chlorine binding site 1 out of 1 in the Functional Domain of Inlj From Listeria Monocytogenes Includes A Cysteine Ladder


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Functional Domain of Inlj From Listeria Monocytogenes Includes A Cysteine Ladder within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2

b:11.7
occ:1.00
OG A:SER61 3.5 14.7 1.0
O A:HOH570 3.5 25.1 1.0
CB A:SER61 3.9 19.9 1.0
CB A:ASN63 4.0 15.6 1.0
CG2 A:THR84 4.2 16.0 1.0
ND2 A:ASN63 4.3 18.2 1.0
CA A:THR84 4.6 17.8 1.0
CB A:THR84 4.6 17.9 1.0
CG A:ASN63 4.7 16.5 1.0

Reference:

M.Bublitz, C.Holland, C.Sabet, J.Reichelt, P.Cossart, D.W.Heinz, H.Bierne, W.D.Schubert. Crystal Structure and Standardized Geometric Analysis of Inlj, A Listerial Virulence Factor and Leucine-Rich Repeat Protein with A Novel Cysteine Ladder. J.Mol.Biol. V. 378 87 2008.
ISSN: ISSN 0022-2836
PubMed: 18343406
DOI: 10.1016/J.JMB.2008.01.100
Page generated: Sat Dec 12 09:33:55 2020

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