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Zinc in PDB 6vvv: Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rifampicin-Resistant Rna Polymerase

Enzymatic activity of Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rifampicin-Resistant Rna Polymerase

All present enzymatic activity of Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rifampicin-Resistant Rna Polymerase:
2.7.7.6;

Protein crystallography data

The structure of Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rifampicin-Resistant Rna Polymerase, PDB code: 6vvv was solved by M.Lilic, 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) 49.83 / 3.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 129.748, 162.344, 137.155, 90.00, 111.27, 90.00
R / Rfree (%) 23.4 / 26.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rifampicin-Resistant Rna Polymerase (pdb code 6vvv). 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 Rifampicin-Resistant Rna Polymerase, PDB code: 6vvv:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6vvv

Go back to Zinc Binding Sites List in 6vvv
Zinc binding site 1 out of 2 in the Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rifampicin-Resistant Rna Polymerase


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 Rifampicin-Resistant Rna Polymerase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1409

b:0.8
occ:1.00
SG D:CYS977 2.2 0.3 1.0
SG D:CYS967 2.3 85.2 1.0
SG D:CYS890 2.3 0.4 1.0
SG D:CYS974 2.3 95.0 1.0
CB D:CYS977 2.8 97.9 1.0
CB D:CYS967 3.1 91.5 1.0
CA D:CYS967 3.4 91.2 1.0
CB D:CYS890 3.6 0.9 1.0
NH1 D:ARG962 3.6 0.7 1.0
CB D:CYS974 3.8 93.0 1.0
CA D:CYS977 4.1 96.4 1.0
N D:THR968 4.1 0.3 1.0
N D:CYS977 4.2 87.8 1.0
C D:CYS967 4.3 96.8 1.0
CG2 D:THR892 4.3 0.4 1.0
N D:CYS890 4.4 99.5 1.0
OG D:SER969 4.5 0.1 1.0
N D:CYS974 4.5 70.1 1.0
N D:CYS967 4.6 71.0 1.0
CA D:CYS890 4.6 0.4 1.0
CZ D:ARG962 4.6 0.2 1.0
CA D:CYS974 4.7 85.7 1.0
NH2 D:ARG962 4.9 0.7 1.0

Zinc binding site 2 out of 2 in 6vvv

Go back to Zinc Binding Sites List in 6vvv
Zinc binding site 2 out of 2 in the Crystal Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with Rifampicin-Resistant Rna Polymerase


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 Rifampicin-Resistant Rna Polymerase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1410

b:0.1
occ:1.00
SG D:CYS78 2.3 0.7 1.0
SG D:CYS62 2.3 0.4 1.0
SG D:CYS75 2.3 0.2 1.0
SG D:CYS60 2.3 0.9 1.0
CB D:CYS75 3.2 0.3 1.0
CB D:CYS60 3.3 0.5 1.0
CB D:CYS78 3.3 0.5 1.0
CB D:CYS62 3.4 0.1 1.0
N D:CYS62 3.5 0.1 1.0
N D:CYS78 3.7 0.8 1.0
CA D:CYS62 3.9 0.5 1.0
N D:GLY63 3.9 0.2 1.0
CA D:CYS78 4.1 0.5 1.0
N D:TYR61 4.2 0.4 1.0
CB D:ARG77 4.3 0.5 1.0
N D:LYS64 4.3 0.4 1.0
C D:CYS62 4.4 0.9 1.0
C D:ARG77 4.5 0.8 1.0
C D:CYS60 4.5 99.0 1.0
CA D:CYS60 4.5 0.8 1.0
CB D:LYS64 4.6 0.0 1.0
C D:TYR61 4.6 0.7 1.0
CA D:CYS75 4.6 94.5 1.0
CA D:ARG77 4.7 0.2 1.0
N D:ARG77 4.8 0.6 1.0
CA D:TYR61 4.9 0.4 1.0
C D:CYS78 5.0 99.5 1.0
C D:CYS75 5.0 0.6 1.0
CA D:GLY63 5.0 0.7 1.0

Reference:

M.Lilic, J.Chen, H.Boyaci, N.Braffman, E.A.Hubin, J.Herrmann, R.Muller, R.Mooney, R.Landick, S.A.Darst, E.A.Campbell. The Antibiotic Sorangicin A Inhibits Promoter Dna Unwinding in A Mycobacterium Tuberculosis Rifampicin-Resistant Rna Polymerase. Proc.Natl.Acad.Sci.Usa 2020.
ISSN: ESSN 1091-6490
PubMed: 33199626
DOI: 10.1073/PNAS.2013706117
Page generated: Tue Oct 29 09:08:35 2024

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