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Chlorine in PDB 2g9f: Crystal Structure of Intein-Tagged Mouse Pngase C-Terminal Domain

Enzymatic activity of Crystal Structure of Intein-Tagged Mouse Pngase C-Terminal Domain

All present enzymatic activity of Crystal Structure of Intein-Tagged Mouse Pngase C-Terminal Domain:
3.5.1.52;

Protein crystallography data

The structure of Crystal Structure of Intein-Tagged Mouse Pngase C-Terminal Domain, PDB code: 2g9f was solved by X.Zhou, G.Zhao, L.Wang, G.Li, W.J.Lennarz, H.Schindelin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 40.760, 40.760, 193.663, 90.00, 90.00, 120.00
R / Rfree (%) 16.7 / 21.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Intein-Tagged Mouse Pngase C-Terminal Domain (pdb code 2g9f). 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 Intein-Tagged Mouse Pngase C-Terminal Domain, PDB code: 2g9f:

Chlorine binding site 1 out of 1 in 2g9f

Go back to Chlorine Binding Sites List in 2g9f
Chlorine binding site 1 out of 1 in the Crystal Structure of Intein-Tagged Mouse Pngase C-Terminal Domain


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 Intein-Tagged Mouse Pngase C-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl101

b:29.5
occ:0.50
OG A:SER616 2.9 35.2 0.5
OG A:SER616 3.5 38.5 0.5
NH2 A:ARG579 3.6 37.5 1.0
NE A:ARG617 3.6 38.3 1.0
NE A:ARG579 3.8 38.0 1.0
O A:HOH3 3.8 21.7 1.0
NH2 A:ARG617 3.9 37.6 1.0
CB A:SER616 3.9 39.2 1.0
CZ A:ARG617 4.1 38.8 1.0
CZ A:ARG579 4.1 38.8 1.0
OG A:SER577 4.4 43.1 1.0
CD A:ARG617 4.4 37.0 1.0
CG A:ARG617 4.4 38.6 1.0
CB A:SER577 4.8 38.1 1.0
CD A:ARG579 4.9 36.3 1.0

Reference:

X.Zhou, G.Zhao, J.J.Truglio, L.Wang, G.Li, W.J.Lennarz, H.Schindelin. Structural and Biochemical Studies of the C-Terminal Domain of Mouse Peptide-N-Glycanase Identify It As A Mannose-Binding Module. Proc.Natl.Acad.Sci.Usa V. 103 17214 2006.
ISSN: ISSN 0027-8424
PubMed: 17088551
DOI: 10.1073/PNAS.0602954103
Page generated: Thu Jul 10 22:18:58 2025

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