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Chlorine in PDB 4quy: Ycp BETA5-A49S-Mutant

Enzymatic activity of Ycp BETA5-A49S-Mutant

All present enzymatic activity of Ycp BETA5-A49S-Mutant:
3.4.25.1;

Protein crystallography data

The structure of Ycp BETA5-A49S-Mutant, PDB code: 4quy was solved by E.M.Huber, W.Heinemeyer, M.Groll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 134.500, 300.140, 144.190, 90.00, 112.83, 90.00
R / Rfree (%) 19.1 / 22.6

Other elements in 4quy:

The structure of Ycp BETA5-A49S-Mutant also contains other interesting chemical elements:

Magnesium (Mg) 8 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Ycp BETA5-A49S-Mutant (pdb code 4quy). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Ycp BETA5-A49S-Mutant, PDB code: 4quy:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 4quy

Go back to Chlorine Binding Sites List in 4quy
Chlorine binding site 1 out of 2 in the Ycp BETA5-A49S-Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Ycp BETA5-A49S-Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cl302

b:46.1
occ:1.00
OH H:TYR69 2.9 44.8 1.0
NH1 G:ARG111 3.0 48.0 1.0
OD1 G:ASN114 3.3 50.8 1.0
CB G:ASN114 3.6 43.9 1.0
CD G:ARG111 3.6 45.5 1.0
CZ H:TYR69 3.7 42.2 1.0
CE2 H:TYR69 3.8 41.6 1.0
CG G:ASN114 3.8 45.3 1.0
CZ G:ARG111 4.0 47.2 1.0
NE G:ARG111 4.3 46.3 1.0
CA G:ARG111 4.6 45.3 1.0
O G:ARG111 4.7 47.4 1.0
CG G:ARG111 4.9 45.1 1.0
OD2 A:ASP87 5.0 53.5 1.0

Chlorine binding site 2 out of 2 in 4quy

Go back to Chlorine Binding Sites List in 4quy
Chlorine binding site 2 out of 2 in the Ycp BETA5-A49S-Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Ycp BETA5-A49S-Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
U:Cl301

b:49.5
occ:1.00
OH V:TYR69 2.8 53.0 1.0
NH1 U:ARG111 3.1 51.6 1.0
OD1 U:ASN114 3.2 53.0 1.0
CB U:ASN114 3.6 49.6 1.0
CZ V:TYR69 3.7 52.5 1.0
CE2 V:TYR69 3.7 54.7 1.0
CD U:ARG111 3.7 51.0 1.0
CG U:ASN114 3.8 52.1 1.0
CZ U:ARG111 4.2 51.6 1.0
NE U:ARG111 4.4 53.0 1.0
CA U:ARG111 4.7 48.5 1.0
O U:HOH411 4.8 38.4 1.0
O U:ARG111 4.8 51.7 1.0
OD2 O:ASP87 4.9 58.3 1.0
CE1 V:TYR69 4.9 53.2 1.0
CD2 V:TYR69 5.0 54.1 1.0
ND2 U:ASN114 5.0 50.6 1.0

Reference:

E.M.Huber, W.Heinemeyer, M.Groll. Bortezomib-Resistant Mutant Proteasomes: Structural and Biochemical Evaluation with Carfilzomib and Onx 0914. Structure 2015.
ISSN: ISSN 0969-2126
PubMed: 25599643
DOI: 10.1016/J.STR.2014.11.019
Page generated: Sat Dec 12 11:06:44 2020

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