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Chlorine in PDB 2g5t: Crystal Structure of Human Dipeptidyl Peptidase IV (Dppiv) Complexed with Cyanopyrrolidine (C5-Pro-Pro) Inhibitor 21AG

Enzymatic activity of Crystal Structure of Human Dipeptidyl Peptidase IV (Dppiv) Complexed with Cyanopyrrolidine (C5-Pro-Pro) Inhibitor 21AG

All present enzymatic activity of Crystal Structure of Human Dipeptidyl Peptidase IV (Dppiv) Complexed with Cyanopyrrolidine (C5-Pro-Pro) Inhibitor 21AG:
3.4.14.5;

Protein crystallography data

The structure of Crystal Structure of Human Dipeptidyl Peptidase IV (Dppiv) Complexed with Cyanopyrrolidine (C5-Pro-Pro) Inhibitor 21AG, PDB code: 2g5t was solved by K.L.Longenecker, E.H.Fry, M.R.Lake, L.R.Solomon, Z.Pei, X.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 65.733, 126.788, 112.292, 90.00, 99.49, 90.00
R / Rfree (%) 19 / 24.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Dipeptidyl Peptidase IV (Dppiv) Complexed with Cyanopyrrolidine (C5-Pro-Pro) Inhibitor 21AG (pdb code 2g5t). 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 Human Dipeptidyl Peptidase IV (Dppiv) Complexed with Cyanopyrrolidine (C5-Pro-Pro) Inhibitor 21AG, PDB code: 2g5t:

Chlorine binding site 1 out of 1 in 2g5t

Go back to Chlorine Binding Sites List in 2g5t
Chlorine binding site 1 out of 1 in the Crystal Structure of Human Dipeptidyl Peptidase IV (Dppiv) Complexed with Cyanopyrrolidine (C5-Pro-Pro) Inhibitor 21AG


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 Human Dipeptidyl Peptidase IV (Dppiv) Complexed with Cyanopyrrolidine (C5-Pro-Pro) Inhibitor 21AG within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl800

b:11.3
occ:1.00
 CL23 A:ACF800 0.0 11.3 1.0
C12 A:ACF800 1.7 20.5 1.0
C13 A:ACF800 2.7 24.0 1.0
C10 A:ACF800 2.7 23.0 1.0
O11 A:ACF800 2.9 22.8 1.0
O A:HOH1204 3.2 31.7 1.0
OH A:TYR547 3.6 16.6 1.0
N22 A:ACF800 3.7 23.2 1.0
C14 A:ACF800 4.0 23.5 1.0
O A:HOH1027 4.0 15.4 1.0
C16 A:ACF800 4.1 23.9 1.0
O A:HOH1273 4.1 35.0 1.0
C4 A:ACF800 4.3 20.8 1.0
O3 A:ACF800 4.3 21.8 1.0
CZ A:TYR547 4.3 21.3 1.0
NH2 A:ARG125 4.3 12.7 1.0
C9 A:ACF800 4.3 21.0 1.0
C1 A:ACF800 4.4 22.6 1.0
CE1 A:TYR547 4.5 20.2 1.0
C15 A:ACF800 4.6 26.9 1.0
O A:HOH1121 4.6 38.0 1.0
NH1 A:ARG125 4.6 12.4 1.0
C2 A:ACF800 4.7 21.9 1.0
C21 A:ACF800 4.7 23.6 1.0
CZ A:ARG125 4.8 13.3 1.0
N7 A:ACF800 4.8 23.3 1.0
C5 A:ACF800 4.9 19.9 1.0
C6 A:ACF800 4.9 20.8 1.0
N8 A:ACF800 5.0 24.3 1.0

Reference:

Z.Pei, X.Li, K.Longenecker, T.W.Von Geldern, P.E.Wiedeman, T.H.Lubben, B.A.Zinker, K.Stewart, S.J.Ballaron, M.A.Stashko, A.K.Mika, D.W.Beno, M.Long, H.Wells, A.J.Kempf-Grote, D.J.Madar, T.S.Mcdermott, L.Bhagavatula, M.G.Fickes, D.Pireh, L.R.Solomon, M.R.Lake, R.Edalji, E.H.Fry, H.L.Sham, J.M.Trevillyan. Discovery, Structure-Activity Relationship, and Pharmacological Evaluation of (5-Substituted-Pyrrolidinyl-2-Carbonyl)-2-Cyanopyrrolidines As Potent Dipeptidyl Peptidase IV Inhibitors. J.Med.Chem. V. 49 3520 2006.
ISSN: ISSN 0022-2623
PubMed: 16759095
DOI: 10.1021/JM051283E
Page generated: Sat Jul 20 07:21:39 2024

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