Zinc in PDB 5tw1: Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rbpa

Enzymatic activity of Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rbpa

All present enzymatic activity of Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rbpa:
2.7.7.6;

Protein crystallography data

The structure of Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rbpa, PDB code: 5tw1 was solved by E.A.Hubin, S.A.Darst, E.A.Campbell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 54.91 / 2.76
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 133.012, 161.633, 139.211, 90.00, 107.72, 90.00
R / Rfree (%) 23.9 / 28

Other elements in 5tw1:

The structure of Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rbpa also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rbpa (pdb code 5tw1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rbpa, PDB code: 5tw1:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5tw1

Go back to Zinc Binding Sites List in 5tw1
Zinc binding site 1 out of 2 in the Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rbpa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rbpa within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn2001

b:66.7
occ:1.00
SG D:CYS977 2.1 57.3 1.0
SG D:CYS967 2.2 59.6 1.0
SG D:CYS974 2.2 53.2 1.0
SG D:CYS890 2.2 60.3 1.0
CB D:CYS977 2.9 55.7 1.0
CB D:CYS967 3.1 56.0 1.0
CB D:CYS974 3.4 54.7 1.0
CB D:CYS890 3.4 62.7 1.0
NH1 D:ARG962 3.5 55.6 1.0
CA D:CYS967 3.6 57.5 1.0
N D:CYS890 4.1 67.4 1.0
CA D:CYS977 4.1 49.3 1.0
N D:CYS974 4.2 47.3 1.0
OG D:SER969 4.2 67.5 1.0
N D:THR968 4.2 61.3 1.0
N D:CYS977 4.2 44.0 1.0
CA D:CYS974 4.3 49.6 1.0
CA D:CYS890 4.3 64.9 1.0
C D:CYS967 4.4 58.8 1.0
CG2 D:THR892 4.5 64.1 1.0
CZ D:ARG962 4.6 47.7 1.0
O D:CYS974 4.6 42.0 1.0
C D:CYS974 4.8 47.2 1.0
N D:SER969 4.8 55.6 1.0
N D:CYS967 4.8 61.3 1.0
NH2 D:ARG962 4.9 65.7 1.0

Zinc binding site 2 out of 2 in 5tw1

Go back to Zinc Binding Sites List in 5tw1
Zinc binding site 2 out of 2 in the Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rbpa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rbpa within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn2002

b:0.9
occ:1.00
SG D:CYS75 1.9 63.6 1.0
SG D:CYS60 2.0 89.1 1.0
SG D:CYS62 2.1 79.4 1.0
SG D:CYS78 2.1 87.3 1.0
CB D:CYS75 2.9 79.2 1.0
CB D:CYS60 3.1 92.6 1.0
CB D:CYS62 3.6 97.7 1.0
CB D:CYS78 3.6 78.0 1.0
N D:CYS62 3.7 86.4 1.0
N D:GLY63 3.8 94.6 1.0
N D:CYS78 4.0 77.8 1.0
CA D:CYS62 4.1 96.6 1.0
N D:LYS64 4.1 91.2 1.0
N D:TYR61 4.3 82.9 1.0
CA D:CYS75 4.3 66.5 1.0
CA D:CYS60 4.4 87.1 1.0
C D:CYS60 4.4 85.4 1.0
C D:CYS62 4.4 89.6 1.0
CA D:CYS78 4.4 75.1 1.0
CB D:LYS64 4.5 94.6 1.0
C D:TYR61 4.7 84.0 1.0
CB D:ARG77 4.8 97.3 1.0
CA D:GLY63 4.8 96.1 1.0
C D:GLY63 4.9 89.8 1.0
CA D:LYS64 4.9 90.6 1.0
C D:CYS75 4.9 79.8 1.0
O D:CYS60 4.9 89.9 1.0
N D:TYR65 5.0 0.7 1.0

Reference:

E.A.Hubin, A.Fay, C.Xu, J.M.Bean, R.M.Saecker, M.S.Glickman, S.A.Darst, E.A.Campbell. Structure and Function of the Mycobacterial Transcription Initiation Complex with the Essential Regulator Rbpa. Elife V. 6 2017.
ISSN: ESSN 2050-084X
PubMed: 28067618
DOI: 10.7554/ELIFE.22520
Page generated: Wed Dec 16 10:57:31 2020

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