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Chlorine in PDB 2rd7: Human Complement Membrane Attack Proteins Share A Common Fold with Bacterial Cytolysins

Protein crystallography data

The structure of Human Complement Membrane Attack Proteins Share A Common Fold with Bacterial Cytolysins, PDB code: 2rd7 was solved by D.J.Slade, L.L.Lovelace, M.Chruszcz, W.Minor, L.Lebioda, J.M.Sodetz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.00 / 2.15
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 96.553, 126.087, 51.887, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 26.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Human Complement Membrane Attack Proteins Share A Common Fold with Bacterial Cytolysins (pdb code 2rd7). 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 Human Complement Membrane Attack Proteins Share A Common Fold with Bacterial Cytolysins, PDB code: 2rd7:

Chlorine binding site 1 out of 1 in 2rd7

Go back to Chlorine Binding Sites List in 2rd7
Chlorine binding site 1 out of 1 in the Human Complement Membrane Attack Proteins Share A Common Fold with Bacterial Cytolysins


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Complement Membrane Attack Proteins Share A Common Fold with Bacterial Cytolysins within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl183

b:57.9
occ:1.00
N C:GLY166 3.6 51.7 1.0
N C:PHE167 4.2 52.6 1.0
CA C:GLY166 4.3 51.1 1.0
C C:TYR165 4.6 50.4 1.0
CA C:TYR165 4.6 50.6 1.0
CB C:TYR165 4.7 51.8 1.0
C C:GLY166 4.7 51.3 1.0
O C:PHE167 4.9 54.5 1.0
CD1 C:PHE167 4.9 52.2 1.0

Reference:

L.L.Lovelace, C.L.Cooper, J.M.Sodetz, L.Lebioda. Structure of Human C8 Protein Provides Mechanistic Insight Into Membrane Pore Formation By Complement. J. Biol. Chem. V. 286 17585 2011.
ISSN: ESSN 1083-351X
PubMed: 21454577
DOI: 10.1074/JBC.M111.219766
Page generated: Fri Jul 11 00:29:29 2025

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