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Chlorine in PDB 3lpp: Crystal Complex of N-Terminal Sucrase-Isomaltase with Kotalanol

Enzymatic activity of Crystal Complex of N-Terminal Sucrase-Isomaltase with Kotalanol

All present enzymatic activity of Crystal Complex of N-Terminal Sucrase-Isomaltase with Kotalanol:
3.2.1.10;

Protein crystallography data

The structure of Crystal Complex of N-Terminal Sucrase-Isomaltase with Kotalanol, PDB code: 3lpp was solved by L.Sim, D.R.Rose, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.95 / 2.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.403, 165.763, 341.400, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 22.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Complex of N-Terminal Sucrase-Isomaltase with Kotalanol (pdb code 3lpp). 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 Complex of N-Terminal Sucrase-Isomaltase with Kotalanol, PDB code: 3lpp:

Chlorine binding site 1 out of 1 in 3lpp

Go back to Chlorine Binding Sites List in 3lpp
Chlorine binding site 1 out of 1 in the Crystal Complex of N-Terminal Sucrase-Isomaltase with Kotalanol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Complex of N-Terminal Sucrase-Isomaltase with Kotalanol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl8001

b:3.4
occ:1.00
N A:SER550 3.1 11.0 1.0
NE1 A:TRP318 3.2 5.0 1.0
O A:HOH1441 3.2 6.1 1.0
O A:HOH1252 3.3 7.1 1.0
CA A:SER550 3.5 10.8 1.0
CB A:GLU803 4.0 13.4 1.0
CD1 A:TRP318 4.0 4.3 1.0
CB A:ALA316 4.0 7.0 1.0
N A:ARG549 4.0 11.2 1.0
CB A:LYS548 4.0 12.6 1.0
CE2 A:TRP318 4.2 3.5 1.0
C A:ARG549 4.2 11.9 1.0
O A:GLU803 4.3 12.6 1.0
O A:SER550 4.4 10.8 1.0
C A:SER550 4.4 10.9 1.0
CA A:GLU803 4.5 13.6 1.0
CA A:ARG549 4.5 11.5 1.0
CZ2 A:TRP318 4.6 3.2 1.0
CB A:SER550 4.7 10.3 1.0
CB A:ARG549 4.8 10.8 1.0
C A:LYS548 4.8 12.2 1.0
CG A:LYS548 4.8 14.8 1.0
CA A:LYS548 4.9 12.3 1.0
C A:GLU803 4.9 13.2 1.0

Reference:

L.Sim, C.Willemsma, S.Mohan, H.Y.Naim, B.M.Pinto, D.R.Rose. Structural Basis For Substrate Selectivity in Human Maltase-Glucoamylase and Sucrase-Isomaltase N-Terminal Domains. J.Biol.Chem. V. 285 17763 2010.
ISSN: ISSN 0021-9258
PubMed: 20356844
DOI: 10.1074/JBC.M109.078980
Page generated: Sat Dec 12 09:53:37 2020

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