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Chlorine in PDB 6z3u: Structure of the Cak Complex Form Chaetomium Thermophilum

Protein crystallography data

The structure of Structure of the Cak Complex Form Chaetomium Thermophilum, PDB code: 6z3u was solved by S.Peissert, J.Kuper, C.Kisker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 75.87 / 2.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 81.436, 85.240, 160.401, 90.00, 96.93, 90.00
R / Rfree (%) 20.3 / 24.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Cak Complex Form Chaetomium Thermophilum (pdb code 6z3u). 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 Structure of the Cak Complex Form Chaetomium Thermophilum, PDB code: 6z3u:

Chlorine binding site 1 out of 1 in 6z3u

Go back to Chlorine Binding Sites List in 6z3u
Chlorine binding site 1 out of 1 in the Structure of the Cak Complex Form Chaetomium Thermophilum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Cak Complex Form Chaetomium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl501

b:17.7
occ:1.00
HE E:ARG191 2.6 28.1 1.0
HH21 B:ARG292 2.7 34.5 1.0
HE B:ARG191 2.7 24.1 1.0
HH21 E:ARG292 2.8 28.6 1.0
H B:TYR192 3.0 30.0 1.0
HH11 B:ARG191 3.0 36.8 1.0
HH11 E:ARG191 3.0 33.5 1.0
H E:TYR192 3.1 23.5 1.0
O B:TYR192 3.2 37.1 1.0
O E:TYR192 3.3 30.7 1.0
NH2 B:ARG292 3.3 28.0 1.0
NH2 E:ARG292 3.4 23.1 1.0
HH22 B:ARG292 3.4 34.5 1.0
HH22 E:ARG292 3.4 28.6 1.0
NE E:ARG191 3.4 24.5 1.0
HA B:ARG191 3.5 31.9 1.0
HA E:ARG191 3.5 21.7 1.0
NE B:ARG191 3.5 23.8 1.0
HD2 B:ARG292 3.6 35.7 1.0
HD2 E:ARG292 3.7 32.0 1.0
NH1 B:ARG191 3.7 30.0 1.0
N B:TYR192 3.8 24.2 1.0
NH1 E:ARG191 3.8 27.2 1.0
N E:TYR192 3.9 19.2 1.0
CZ E:ARG191 4.1 24.7 1.0
CZ B:ARG191 4.1 24.1 1.0
C B:TYR192 4.2 31.8 1.0
HD3 E:ARG191 4.3 32.2 1.0
CA B:ARG191 4.3 25.9 1.0
C E:TYR192 4.4 27.7 1.0
CA E:ARG191 4.4 21.7 1.0
HB3 E:ARG191 4.4 26.6 1.0
CD B:ARG292 4.4 29.0 1.0
HD3 B:ARG191 4.4 26.4 1.0
HH12 B:ARG191 4.5 36.8 1.0
CD E:ARG191 4.5 26.1 1.0
HB3 B:ARG191 4.5 32.8 1.0
HH12 E:ARG191 4.5 33.5 1.0
CZ B:ARG292 4.5 20.4 1.0
HD3 B:ARG292 4.5 35.7 1.0
CD E:ARG292 4.6 25.9 1.0
C B:ARG191 4.6 25.8 1.0
CZ E:ARG292 4.6 20.8 1.0
CD B:ARG191 4.6 24.5 1.0
CA B:TYR192 4.6 27.1 1.0
C E:ARG191 4.7 20.3 1.0
HD3 E:ARG292 4.7 32.0 1.0
O B:VAL190 4.8 29.7 1.0
CA E:TYR192 4.8 22.6 1.0
O E:VAL190 4.8 21.0 1.0
CB E:ARG191 4.9 23.7 1.0
CB B:ARG191 4.9 26.6 1.0
NE B:ARG292 5.0 20.2 1.0

Reference:

S.Peissert, A.Schlosser, R.Kendel, J.Kuper, C.Kisker. Structural Basis For CDK7 Activation By MAT1 and Cyclin H. Proc.Natl.Acad.Sci.Usa V. 117 26739 2020.
ISSN: ESSN 1091-6490
PubMed: 33055219
DOI: 10.1073/PNAS.2010885117
Page generated: Mon Jul 29 17:56:50 2024

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