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Chlorine in PDB 2xzr: Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors

Protein crystallography data

The structure of Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors, PDB code: 2xzr was solved by M.D.Hartmann, B.Hernandez Alvarez, O.Ridderbusch, S.Deiss, A.N.Lupas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.10 / 2.80
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 36.670, 36.670, 228.580, 90.00, 90.00, 120.00
R / Rfree (%) 25.967 / 30.775

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors (pdb code 2xzr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors, PDB code: 2xzr:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 2xzr

Go back to Chlorine Binding Sites List in 2xzr
Chlorine binding site 1 out of 4 in the Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1001

b:64.0
occ:0.33
ND2 A:ASN400 3.5 60.9 1.0
CB A:ASN400 3.9 58.7 1.0
CG2 A:VAL397 4.2 52.3 1.0
CG A:ASN400 4.2 61.7 1.0
CA A:VAL397 4.4 52.8 1.0
CG1 A:VAL397 4.4 53.2 1.0
CB A:VAL397 4.5 52.6 1.0
O A:VAL397 4.8 53.9 1.0

Chlorine binding site 2 out of 4 in 2xzr

Go back to Chlorine Binding Sites List in 2xzr
Chlorine binding site 2 out of 4 in the Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1002

b:42.9
occ:0.33
ND2 A:ASN407 2.9 52.3 1.0
CB A:ASN407 3.8 49.3 1.0
CG A:ASN407 3.8 52.2 1.0
CA A:ILE404 4.4 60.0 1.0
CG1 A:ILE404 4.4 62.4 1.0
CG2 A:ILE404 4.4 63.5 1.0
CB A:ILE404 4.6 62.5 1.0
O A:ILE404 4.9 59.1 1.0

Chlorine binding site 3 out of 4 in 2xzr

Go back to Chlorine Binding Sites List in 2xzr
Chlorine binding site 3 out of 4 in the Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1003

b:44.6
occ:0.33
ND2 A:ASN414 3.6 53.9 1.0
CB A:ASN414 4.1 47.7 1.0
CG A:ASN414 4.3 52.1 1.0
CG2 A:ILE411 4.4 51.0 1.0
CG1 A:ILE411 4.4 46.6 1.0
CA A:ILE411 4.5 48.2 1.0
CB A:ILE411 4.7 48.2 1.0

Chlorine binding site 4 out of 4 in 2xzr

Go back to Chlorine Binding Sites List in 2xzr
Chlorine binding site 4 out of 4 in the Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Escherichia Coli Immunoglobulin-Binding Protein Eibd 391-438 Fused to GCN4 Adaptors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1004

b:34.9
occ:0.33
ND2 A:ASN435 3.5 39.7 1.0
CB A:ASN435 3.9 37.6 1.0
CG A:ASN435 4.2 40.9 1.0
CA A:ILE432 4.4 40.2 1.0
CG2 A:ILE432 4.4 46.7 1.0
CG1 A:ILE432 4.5 45.3 1.0
CB A:ILE432 4.7 44.9 1.0
O A:ILE432 5.0 39.5 1.0

Reference:

J.C.Leo, A.Lyskowski, K.Hattula, M.D.Hartmann, H.Schwarz, S.J.Butcher, D.Linke, A.N.Lupas, A.Goldman. The Structure of E. Coli Igg-Binding Protein D Suggests A General Model For Bending and Binding in Trimeric Autotransporter Adhesins. Structure V. 19 1021 2011.
ISSN: ISSN 0969-2126
PubMed: 21742268
DOI: 10.1016/J.STR.2011.03.021
Page generated: Fri Jul 11 02:13:50 2025

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