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Chlorine in PDB 4qo0: Crystal Structure of Rhomboid Intramembrane Protease Glpg in Complex with Peptide Derived Inhibitor Ac-Fata-Cmk

Enzymatic activity of Crystal Structure of Rhomboid Intramembrane Protease Glpg in Complex with Peptide Derived Inhibitor Ac-Fata-Cmk

All present enzymatic activity of Crystal Structure of Rhomboid Intramembrane Protease Glpg in Complex with Peptide Derived Inhibitor Ac-Fata-Cmk:
3.4.21.105;

Protein crystallography data

The structure of Crystal Structure of Rhomboid Intramembrane Protease Glpg in Complex with Peptide Derived Inhibitor Ac-Fata-Cmk, PDB code: 4qo0 was solved by S.Zoll, K.Strisovsky, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.79 / 2.90
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 98.310, 98.310, 65.250, 90.00, 90.00, 120.00
R / Rfree (%) 18.2 / 22.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Rhomboid Intramembrane Protease Glpg in Complex with Peptide Derived Inhibitor Ac-Fata-Cmk (pdb code 4qo0). 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 Rhomboid Intramembrane Protease Glpg in Complex with Peptide Derived Inhibitor Ac-Fata-Cmk, PDB code: 4qo0:

Chlorine binding site 1 out of 1 in 4qo0

Go back to Chlorine Binding Sites List in 4qo0
Chlorine binding site 1 out of 1 in the Crystal Structure of Rhomboid Intramembrane Protease Glpg in Complex with Peptide Derived Inhibitor Ac-Fata-Cmk


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 Rhomboid Intramembrane Protease Glpg in Complex with Peptide Derived Inhibitor Ac-Fata-Cmk within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:59.7
occ:1.00
 OG1 F:THR4 3.1 47.5 1.0
N A:PHE146 3.2 46.3 1.0
CB A:HIS150 3.4 43.0 1.0
CB F:THR4 3.5 47.9 1.0
N A:SER147 3.5 46.5 1.0
OG A:SER147 3.6 44.1 1.0
CA A:HIS145 3.9 48.1 1.0
CB A:HIS145 4.0 46.7 1.0
C A:HIS145 4.0 45.9 1.0
CD2 A:PHE146 4.0 52.7 1.0
CD2 A:HIS145 4.0 45.4 1.0
CA A:PHE146 4.1 46.2 1.0
CG2 F:THR4 4.1 45.6 1.0
O A:SER147 4.1 46.8 1.0
CB A:SER147 4.1 48.2 1.0
CG A:HIS150 4.2 48.7 1.0
C A:PHE146 4.2 46.8 1.0
CB A:PHE146 4.3 43.9 1.0
CA A:SER147 4.3 48.6 1.0
CG A:HIS145 4.4 45.6 1.0
ND1 A:HIS150 4.5 48.4 1.0
CG A:PHE146 4.5 53.0 1.0
CA A:HIS150 4.6 44.9 1.0
C A:SER147 4.7 47.8 1.0
CA F:THR4 4.8 49.8 1.0
CE2 A:PHE146 4.9 52.4 1.0
N A:ILE151 4.9 42.2 1.0
C A:HIS150 4.9 42.9 1.0

Reference:

S.Zoll, S.Stanchev, J.Began, J.Skerle, M.Lepsik, L.Peclinovska, P.Majer, K.Strisovsky. Substrate Binding and Specificity of Rhomboid Intramembrane Protease Revealed By Substrate-Peptide Complex Structures. Embo J. V. 33 2408 2014.
ISSN: ISSN 0261-4189
PubMed: 25216680
DOI: 10.15252/EMBJ.201489367
Page generated: Fri Jul 26 00:35:12 2024

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