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Chlorine in PDB 7ubj: Transcription Antitermination Factor Qlambda, Type-I Crystal

Protein crystallography data

The structure of Transcription Antitermination Factor Qlambda, Type-I Crystal, PDB code: 7ubj was solved by Z.Yin, R.H.Ebright, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.27 / 1.46
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 54.341, 54.341, 110.09, 90, 90, 120
R / Rfree (%) 17.8 / 20.3

Other elements in 7ubj:

The structure of Transcription Antitermination Factor Qlambda, Type-I Crystal also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Transcription Antitermination Factor Qlambda, Type-I Crystal (pdb code 7ubj). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Transcription Antitermination Factor Qlambda, Type-I Crystal, PDB code: 7ubj:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 7ubj

Go back to Chlorine Binding Sites List in 7ubj
Chlorine binding site 1 out of 3 in the Transcription Antitermination Factor Qlambda, Type-I Crystal


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Transcription Antitermination Factor Qlambda, Type-I Crystal within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:36.4
occ:1.00
HE1 A:TRP176 2.2 14.8 1.0
HE21 A:GLN173 2.4 30.2 0.5
NE1 A:TRP176 3.0 12.3 1.0
HE21 A:GLN173 3.0 24.6 0.5
HE2 A:LYS181 3.1 36.7 1.0
O A:HOH469 3.1 35.8 1.0
NE2 A:GLN173 3.2 25.1 0.5
HD2 A:LYS181 3.3 23.2 1.0
HB3 A:ALA157 3.4 19.6 1.0
HE22 A:GLN173 3.4 30.2 0.5
HE3 A:LYS181 3.4 36.7 1.0
CE A:LYS181 3.6 30.6 1.0
HA A:SER158 3.6 14.3 0.3
HD1 A:TRP176 3.6 15.7 1.0
HA A:SER158 3.6 14.2 0.7
HB1 A:ALA157 3.7 19.6 1.0
CD1 A:TRP176 3.7 13.1 1.0
NE2 A:GLN173 3.8 20.5 0.5
CD A:LYS181 3.9 19.3 1.0
CB A:ALA157 4.0 16.3 1.0
CE2 A:TRP176 4.1 12.4 1.0
HB2 A:TYR161 4.1 11.3 1.0
HE22 A:GLN173 4.1 24.6 0.5
C A:ALA157 4.2 16.9 1.0
HG3 A:GLN173 4.2 29.8 0.5
HZ2 A:TRP176 4.2 15.7 1.0
N A:SER158 4.2 15.4 1.0
HG2 A:GLN173 4.2 29.0 0.5
O A:HOH601 4.2 43.4 1.0
O A:ALA157 4.3 16.7 1.0
CA A:SER158 4.3 11.9 0.3
CA A:SER158 4.3 11.8 0.7
CD A:GLN173 4.4 26.0 0.5
O A:HOH592 4.4 41.2 1.0
H A:SER158 4.5 18.5 0.7
H A:SER158 4.5 18.5 0.3
HB2 A:SER158 4.5 23.4 0.3
HG3 A:LYS181 4.5 14.4 1.0
HB3 A:SER158 4.5 23.4 0.7
CZ2 A:TRP176 4.5 13.1 1.0
HB3 A:TYR161 4.6 11.3 1.0
CG A:GLN173 4.6 24.8 0.5
HG2 A:GLN173 4.6 29.8 0.5
HD3 A:LYS181 4.7 23.2 1.0
CA A:ALA157 4.7 19.4 1.0
HB2 A:ALA157 4.8 19.6 1.0
CB A:TYR161 4.8 9.4 1.0
CD A:GLN173 4.8 22.0 0.5
CG A:LYS181 4.8 11.9 1.0
CG A:GLN173 4.8 24.1 0.5
HG3 A:GLN173 4.9 29.0 0.5
HB2 A:LYS181 4.9 13.6 1.0
CB A:SER158 4.9 19.5 0.3
CG A:TRP176 5.0 13.3 1.0

Chlorine binding site 2 out of 3 in 7ubj

Go back to Chlorine Binding Sites List in 7ubj
Chlorine binding site 2 out of 3 in the Transcription Antitermination Factor Qlambda, Type-I Crystal


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Transcription Antitermination Factor Qlambda, Type-I Crystal within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl303

b:60.5
occ:1.00
HH22 B:ARG138 2.6 38.0 1.0
HH12 B:ARG138 3.1 54.3 1.0
NH2 B:ARG138 3.4 31.6 1.0
NH1 B:ARG138 3.8 45.2 1.0
HH21 B:ARG138 3.9 38.0 1.0
CZ B:ARG138 4.0 48.7 1.0
CL B:CL304 4.1 62.7 1.0
HH11 B:ARG138 4.5 54.3 1.0

Chlorine binding site 3 out of 3 in 7ubj

Go back to Chlorine Binding Sites List in 7ubj
Chlorine binding site 3 out of 3 in the Transcription Antitermination Factor Qlambda, Type-I Crystal


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Transcription Antitermination Factor Qlambda, Type-I Crystal within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl304

b:62.7
occ:1.00
H B:GLU141 2.2 17.7 1.0
HB2 B:GLU141 3.0 22.0 1.0
HA B:VAL140 3.1 16.2 1.0
HH21 B:ARG138 3.1 38.0 1.0
N B:GLU141 3.1 14.8 1.0
HG13 B:VAL140 3.3 19.2 1.0
HH22 B:ARG138 3.3 38.0 1.0
O B:HOH520 3.4 38.5 1.0
NH2 B:ARG138 3.5 31.6 1.0
CB B:GLU141 3.8 18.3 1.0
CA B:VAL140 3.9 13.5 1.0
HG3 B:GLU141 3.9 27.1 1.0
CA B:GLU141 3.9 16.6 1.0
C B:VAL140 4.0 17.4 1.0
HH21 B:ARG126 4.0 35.1 1.0
CL B:CL303 4.1 60.5 1.0
CG1 B:VAL140 4.2 16.0 1.0
O B:GLU141 4.2 20.9 1.0
CG B:GLU141 4.3 22.6 1.0
HG12 B:VAL140 4.4 19.2 1.0
C B:GLU141 4.5 21.2 1.0
O B:VAL139 4.5 21.0 1.0
OE1 B:GLU141 4.5 29.6 1.0
HB3 B:GLU141 4.6 22.0 1.0
CB B:VAL140 4.6 13.4 1.0
CZ B:ARG138 4.7 48.7 1.0
HG22 B:VAL140 4.8 19.2 1.0
NH2 B:ARG126 4.8 29.2 1.0
CD B:GLU141 4.8 36.3 1.0
HA B:GLU141 4.8 20.0 1.0
HG11 B:VAL140 4.9 19.2 1.0
N B:VAL140 5.0 14.9 1.0
HH22 B:ARG126 5.0 35.1 1.0

Reference:

Z.Yin, J.G.Bird, J.T.Kaelber, B.E.Nickels, R.H.Ebright. In Transcription Antitermination By Q Lambda , Nusa Induces Refolding of Q Lambda to Form A Nozzle That Extends the Rna Polymerase Rna-Exit Channel. Proc.Natl.Acad.Sci.Usa V. 119 78119 2022.
ISSN: ESSN 1091-6490
PubMed: 35951650
DOI: 10.1073/PNAS.2205278119
Page generated: Sun Jul 13 07:45:25 2025

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