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Chlorine in PDB 5jh2: Crystal Structure of the Holo Form of AKR4C7 From Maize

Protein crystallography data

The structure of Crystal Structure of the Holo Form of AKR4C7 From Maize, PDB code: 5jh2 was solved by P.O.Giuseppe, M.L.Santos, S.M.Sousa, K.E.Koch, J.A.Yunes, R.Aparicio, M.T.Murakami, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.39 / 1.72
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.219, 55.857, 105.740, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 20.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Holo Form of AKR4C7 From Maize (pdb code 5jh2). 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 the Holo Form of AKR4C7 From Maize, PDB code: 5jh2:

Chlorine binding site 1 out of 1 in 5jh2

Go back to Chlorine Binding Sites List in 5jh2
Chlorine binding site 1 out of 1 in the Crystal Structure of the Holo Form of AKR4C7 From Maize


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 the Holo Form of AKR4C7 From Maize within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:28.3
occ:1.00
O A:HOH593 3.0 24.0 1.0
N A:TRP80 3.2 22.6 1.0
NH1 A:ARG47 3.6 53.5 1.0
CD A:ARG47 3.7 44.8 1.0
CG A:ARG47 3.7 36.9 1.0
O A:TRP80 3.8 27.1 1.0
CB A:TRP80 3.9 33.1 1.0
CD1 A:LEU79 3.9 28.5 1.0
CA A:TRP80 4.0 26.5 1.0
CB A:VAL48 4.1 27.7 1.0
CA A:LEU79 4.1 23.5 1.0
C A:LEU79 4.1 22.7 1.0
N A:VAL48 4.2 27.4 1.0
C A:TRP80 4.3 26.3 1.0
CA A:VAL48 4.4 28.2 1.0
CZ A:ARG47 4.5 51.0 1.0
NE A:ARG47 4.5 51.8 1.0
O A:LYS78 4.6 26.4 1.0
CG2 A:VAL48 4.7 30.1 1.0
O A:HOH689 4.8 41.0 1.0
CG A:LEU79 4.8 29.1 1.0
CB A:LEU79 4.9 24.3 1.0
C A:ARG47 4.9 24.8 1.0
CB A:ARG47 5.0 33.1 1.0

Reference:

P.O.Giuseppe, M.L.Santos, S.M.Sousa, K.E.Koch, J.A.Yunes, R.Aparicio, M.T.Murakami. A Comparative Structural Analysis Reveals Distinctive Features of Co-Factor Binding and Substrate Specificity in Plant Aldo-Keto Reductases. Biochem.Biophys.Res.Commun. V. 474 696 2016.
ISSN: ESSN 1090-2104
PubMed: 27154221
DOI: 10.1016/J.BBRC.2016.05.011
Page generated: Sat Jul 12 03:37:36 2025

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