Chlorine in PDB 6ieh: Crystal Structures of the HMTR4-NRDE2 Complex

Enzymatic activity of Crystal Structures of the HMTR4-NRDE2 Complex

All present enzymatic activity of Crystal Structures of the HMTR4-NRDE2 Complex:
3.6.4.13;

Protein crystallography data

The structure of Crystal Structures of the HMTR4-NRDE2 Complex, PDB code: 6ieh was solved by J.Y.Chen, C.H.Yun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.10 / 2.89
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 148.305, 113.728, 80.717, 90.00, 96.49, 90.00
R / Rfree (%) 23.6 / 25.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structures of the HMTR4-NRDE2 Complex (pdb code 6ieh). 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 Structures of the HMTR4-NRDE2 Complex, PDB code: 6ieh:

Chlorine binding site 1 out of 1 in 6ieh

Go back to Chlorine Binding Sites List in 6ieh
Chlorine binding site 1 out of 1 in the Crystal Structures of the HMTR4-NRDE2 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structures of the HMTR4-NRDE2 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1101

b:52.2
occ:1.00
CB B:ARG756 3.2 44.3 1.0
O B:LEU750 3.4 44.0 1.0
O B:MET726 3.5 37.8 1.0
O B:ARG751 3.7 46.3 1.0
O B:PRO752 3.7 51.2 1.0
C B:PRO752 4.1 54.6 1.0
CA B:VAL753 4.2 51.7 1.0
C B:ARG751 4.2 43.0 1.0
N B:VAL753 4.4 54.9 1.0
C B:LEU750 4.5 39.0 1.0
CA B:ARG756 4.6 45.7 1.0
C B:MET726 4.6 39.6 1.0
N B:PRO752 4.8 37.4 1.0
CA B:ARG751 4.8 41.2 1.0
O B:VAL753 4.9 54.7 1.0
N B:ARG756 4.9 47.5 1.0
C B:VAL753 4.9 51.8 1.0

Reference:

J.Wang, J.Chen, G.Wu, H.Zhang, X.Du, S.Chen, L.Zhang, K.Wang, J.Fan, S.Gao, X.Wu, S.Zhang, B.Kuai, P.Zhao, B.Chi, L.Wang, G.Li, C.C.L.Wong, Y.Zhou, J.Li, C.Yun, H.Cheng. NRDE2 Negatively Regulates Exosome Functions By Inhibiting MTR4 Recruitment and Exosome Interaction. Genes Dev. V. 33 536 2019.
ISSN: ISSN 0890-9369
PubMed: 30842217
DOI: 10.1101/GAD.322602.118
Page generated: Sat Dec 12 13:10:13 2020

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