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Chlorine in PDB 5di0: Crystal Structure of DLN1

Protein crystallography data

The structure of Crystal Structure of DLN1, PDB code: 5di0 was solved by N.Jia, Y.L.Jiang, W.Cheng, H.W.Wang, C.Z.Zhou, Y.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.60 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.111, 95.100, 147.406, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 20.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of DLN1 (pdb code 5di0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of DLN1, PDB code: 5di0:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5di0

Go back to Chlorine Binding Sites List in 5di0
Chlorine binding site 1 out of 2 in the Crystal Structure of DLN1


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 DLN1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl418

b:25.0
occ:1.00
O2 A:EDO403 2.6 39.9 1.0
O A:HOH739 3.0 26.6 1.0
N A:GLY85 3.1 24.2 1.0
N A:GLY83 3.2 20.0 1.0
CA A:GLY85 3.5 22.8 1.0
CA A:GLY83 3.6 23.2 1.0
CA A:GLY81 3.6 15.8 1.0
C2 A:EDO403 3.6 36.2 1.0
C A:GLY83 3.7 23.9 1.0
N A:ALA84 3.7 23.4 1.0
N A:ASN82 3.7 16.9 1.0
C A:GLY81 3.9 15.8 1.0
O A:HOH837 4.0 48.2 1.0
OD1 A:ASN82 4.1 18.5 1.0
O A:HOH529 4.1 17.8 1.0
O A:GLY83 4.2 27.2 1.0
C A:ALA84 4.2 25.4 1.0
C A:ASN82 4.3 19.8 1.0
N A:GLY81 4.4 15.3 1.0
C A:GLY85 4.6 22.6 1.0
CA A:ALA84 4.6 24.0 1.0
CA A:ASN82 4.7 17.4 1.0
C1 A:EDO403 4.7 32.5 1.0
O A:GLY81 4.8 15.3 1.0
N A:THR86 4.9 19.2 1.0
O A:HOH551 4.9 28.2 1.0
O A:ARG87 4.9 15.2 1.0

Chlorine binding site 2 out of 2 in 5di0

Go back to Chlorine Binding Sites List in 5di0
Chlorine binding site 2 out of 2 in the Crystal Structure of DLN1


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 DLN1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl417

b:29.2
occ:1.00
O2 B:EDO402 2.9 32.1 1.0
N B:GLY83 3.0 17.8 1.0
O B:HOH845 3.1 26.3 1.0
N B:GLY85 3.2 22.8 1.0
CA B:GLY85 3.4 21.0 1.0
CA B:GLY83 3.5 19.4 1.0
CA B:GLY81 3.5 14.2 1.0
C B:GLY83 3.6 20.7 1.0
N B:ASN82 3.6 15.1 1.0
C2 B:EDO402 3.7 33.3 1.0
C B:GLY81 3.8 15.1 1.0
O B:GLY83 3.9 21.6 1.0
O B:HOH565 3.9 16.5 1.0
N B:ALA84 4.0 21.3 1.0
C B:ASN82 4.1 18.0 1.0
OD1 B:ASN82 4.2 16.2 1.0
N B:GLY81 4.3 14.4 1.0
C B:ALA84 4.4 23.4 1.0
O B:HOH807 4.4 35.4 1.0
CA B:ASN82 4.5 16.0 1.0
O B:GLY81 4.6 15.6 1.0
C B:GLY85 4.7 21.1 1.0
CA B:ALA84 4.8 22.4 1.0
O B:HOH636 4.9 20.4 1.0
C1 B:EDO402 4.9 30.4 1.0

Reference:

N.Jia, N.Liu, W.Cheng, Y.L.Jiang, H.Sun, L.L.Chen, J.Peng, Y.Zhang, Y.H.Ding, Z.H.Zhang, X.Wang, G.Cai, J.Wang, M.Q.Dong, Z.Zhang, H.Wu, H.W.Wang, Y.Chen, C.Z.Zhou. Structural Basis For Receptor Recognition and Pore Formation of A Zebrafish Aerolysin-Like Protein. Embo Rep. V. 17 235 2016.
ISSN: ESSN 1469-3178
PubMed: 26711430
DOI: 10.15252/EMBR.201540851
Page generated: Sat Jul 12 01:16:35 2025

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