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Chlorine in PDB 5t5x: High Resolution Structure of Mouse Cryptochrome 1

Protein crystallography data

The structure of High Resolution Structure of Mouse Cryptochrome 1, PDB code: 5t5x was solved by A.K.Michael, S.Tripathi, C.L.Partch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.43 / 1.84
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 43.630, 51.035, 54.175, 71.62, 84.12, 88.89
R / Rfree (%) 16.8 / 23.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the High Resolution Structure of Mouse Cryptochrome 1 (pdb code 5t5x). 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 High Resolution Structure of Mouse Cryptochrome 1, PDB code: 5t5x:

Chlorine binding site 1 out of 1 in 5t5x

Go back to Chlorine Binding Sites List in 5t5x
Chlorine binding site 1 out of 1 in the High Resolution Structure of Mouse Cryptochrome 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of High Resolution Structure of Mouse Cryptochrome 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl501

b:24.9
occ:1.00
HD1 A:HIS130 1.9 12.2 1.0
HH12 A:ARG14 2.1 9.1 1.0
H A:GLY12 2.5 6.6 1.0
HA A:HIS130 2.6 9.2 1.0
HA2 A:GLY12 2.8 8.1 1.0
ND1 A:HIS130 2.8 10.2 1.0
HA3 A:GLY258 2.8 10.7 1.0
OE2 A:GLU99 2.8 10.1 1.0
NH1 A:ARG14 2.9 7.6 1.0
HA2 A:GLY258 3.0 10.7 1.0
HH11 A:ARG14 3.2 9.1 1.0
N A:GLY12 3.2 5.5 1.0
OE1 A:GLU99 3.2 11.9 1.0
CA A:GLY258 3.3 8.9 1.0
CA A:GLY12 3.4 6.7 1.0
HB2 A:HIS130 3.4 14.3 1.0
CD A:GLU99 3.4 8.7 1.0
O A:HOH787 3.5 11.9 1.0
CA A:HIS130 3.5 7.7 1.0
CG A:HIS130 3.6 17.1 1.0
O A:HOH746 3.7 8.1 1.0
CB A:HIS130 3.7 11.9 1.0
HH22 A:ARG14 3.7 10.2 1.0
HA3 A:GLY12 3.7 8.1 1.0
HB3 A:LYS11 3.8 13.4 1.0
CE1 A:HIS130 3.8 14.8 1.0
CZ A:ARG14 3.9 9.9 1.0
HE1 A:HIS130 4.0 17.7 1.0
O A:SER129 4.0 9.2 0.2
HB2 A:LYS11 4.0 13.4 1.0
O A:SER129 4.1 8.9 0.8
NH2 A:ARG14 4.2 8.5 1.0
N A:HIS130 4.2 6.8 1.0
N A:GLY258 4.3 8.9 1.0
CB A:LYS11 4.3 11.1 1.0
C A:LYS11 4.3 5.8 1.0
C A:GLY258 4.4 12.7 1.0
C A:SER129 4.4 10.6 0.2
O A:GLY258 4.4 8.5 1.0
C A:SER129 4.4 10.7 0.8
C A:HIS130 4.6 13.1 1.0
H A:GLY258 4.6 10.7 1.0
HB3 A:HIS130 4.6 14.3 1.0
HH22 A:ARG293 4.7 13.4 1.0
O A:HIS130 4.7 9.0 1.0
C A:GLY12 4.7 10.6 1.0
H A:HIS130 4.7 8.2 0.8
H A:HIS130 4.7 8.2 0.2
H A:LEU13 4.7 9.9 1.0
HG A:SER129 4.8 12.6 0.8
CD2 A:HIS130 4.8 10.8 1.0
O A:HOH664 4.9 16.8 1.0
CG A:GLU99 4.9 11.1 1.0
NE2 A:HIS130 4.9 9.6 1.0
O A:PHE257 4.9 11.1 1.0
C A:PHE257 4.9 6.6 1.0
HA A:SER261 4.9 17.3 1.0
CA A:LYS11 4.9 5.3 1.0
O A:LEU255 5.0 12.3 1.0

Reference:

A.K.Michael, J.L.Fribourgh, Y.Chelliah, C.R.Sandate, G.L.Hura, D.Schneidman-Duhovny, S.M.Tripathi, J.S.Takahashi, C.L.Partch. Formation of A Repressive Complex in the Mammalian Circadian Clock Is Mediated By the Secondary Pocket of CRY1. Proc. Natl. Acad. Sci. V. 114 1560 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28143926
DOI: 10.1073/PNAS.1615310114
Page generated: Fri Jul 26 17:19:07 2024

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