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Chlorine in PDB 5hgi: Crystal Structure of Apo Human IRE1 Alpha

Enzymatic activity of Crystal Structure of Apo Human IRE1 Alpha

All present enzymatic activity of Crystal Structure of Apo Human IRE1 Alpha:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of Apo Human IRE1 Alpha, PDB code: 5hgi was solved by H.C.Feldman, M.Tong, L.Wang, R.Meza-Acevedo, T.A.Gobillot, J.M.Gliedt, S.B.Hari, A.K.Mitra, B.J.Backes, F.R.Papa, M.A.Seeliger, D.J.Maly, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.34 / 2.58
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 68.039, 169.196, 104.138, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 24.8

Other elements in 5hgi:

The structure of Crystal Structure of Apo Human IRE1 Alpha also contains other interesting chemical elements:

Caesium (Cs) 5 atoms
Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Apo Human IRE1 Alpha (pdb code 5hgi). 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 Apo Human IRE1 Alpha, PDB code: 5hgi:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5hgi

Go back to Chlorine Binding Sites List in 5hgi
Chlorine binding site 1 out of 2 in the Crystal Structure of Apo Human IRE1 Alpha


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 Apo Human IRE1 Alpha within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1012

b:92.8
occ:0.92
O A:HOH1110 3.9 70.5 1.0
CS A:CS1002 4.0 0.3 1.0

Chlorine binding site 2 out of 2 in 5hgi

Go back to Chlorine Binding Sites List in 5hgi
Chlorine binding site 2 out of 2 in the Crystal Structure of Apo Human IRE1 Alpha


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 Apo Human IRE1 Alpha within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1013

b:0.6
occ:1.00
NZ A:LYS704 3.1 0.8 1.0
CE A:LYS704 3.5 1.0 1.0
O A:GLY703 4.1 81.9 1.0
CD A:LYS704 4.3 93.5 1.0
C A:GLY703 4.9 73.9 1.0
CA A:LYS704 5.0 69.7 1.0

Reference:

H.C.Feldman, M.Tong, L.Wang, R.Meza-Acevedo, T.A.Gobillot, I.Lebedev, M.J.Gliedt, S.B.Hari, A.K.Mitra, B.J.Backes, F.R.Papa, M.A.Seeliger, D.J.Maly. Structural and Functional Analysis of the Allosteric Inhibition of IRE1 Alpha with Atp-Competitive Ligands. Acs Chem.Biol. V. 11 2195 2016.
ISSN: ESSN 1554-8937
PubMed: 27227314
DOI: 10.1021/ACSCHEMBIO.5B00940
Page generated: Fri Jul 26 08:49:45 2024

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