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Zinc in PDB 6ccv: Crystal Structure of A Mycobacterium Smegmatis Rna Polymerase Transcription Initiation Complex with Inhibitor Rifampicin

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

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

Protein crystallography data

The structure of Crystal Structure of A Mycobacterium Smegmatis Rna Polymerase Transcription Initiation Complex with Inhibitor Rifampicin, PDB code: 6ccv 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) 57.12 / 3.05
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 132.353, 162.325, 139.401, 90.00, 107.37, 90.00
R / Rfree (%) 22.3 / 26.9

Zinc Binding Sites:

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

Zinc binding site 1 out of 2 in 6ccv

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


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 Rna Polymerase Transcription Initiation Complex with Inhibitor Rifampicin within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn2001

b:0.0
occ:1.00
SG D:CYS977 2.1 59.5 1.0
SG D:CYS890 2.1 91.6 1.0
SG D:CYS974 2.2 81.2 1.0
SG D:CYS967 2.2 76.4 1.0
CB D:CYS890 3.2 83.0 1.0
CB D:CYS977 3.2 74.9 1.0
CB D:CYS967 3.3 56.0 1.0
CB D:CYS974 3.3 70.4 1.0
NH1 D:ARG962 3.5 76.5 1.0
CA D:CYS967 3.8 78.3 1.0
N D:CYS890 3.9 72.1 1.0
OG D:SER969 4.0 0.7 1.0
N D:CYS974 4.1 52.7 1.0
CA D:CYS890 4.1 65.2 1.0
N D:THR968 4.2 76.4 1.0
CA D:CYS974 4.3 59.2 1.0
N D:CYS977 4.3 51.3 1.0
CA D:CYS977 4.3 58.9 1.0
C D:CYS967 4.5 68.9 1.0
CZ D:ARG962 4.6 50.1 1.0
CG2 D:THR892 4.6 76.7 1.0
NH2 D:ARG962 4.7 58.5 1.0
O D:CYS974 4.8 48.3 1.0
N D:SER969 4.8 83.8 1.0
C D:CYS974 4.9 62.0 1.0
C D:CYS890 5.0 76.6 1.0
N D:CYS967 5.0 67.6 1.0

Zinc binding site 2 out of 2 in 6ccv

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


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 Rna Polymerase Transcription Initiation Complex with Inhibitor Rifampicin within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn2002

b:0.7
occ:1.00
SG D:CYS62 2.2 76.5 1.0
SG D:CYS75 2.2 83.5 1.0
SG D:CYS60 2.2 0.8 1.0
SG D:CYS78 2.3 0.7 1.0
CB D:CYS75 2.9 83.4 1.0
CB D:CYS60 3.2 89.9 1.0
CB D:CYS78 3.7 0.5 1.0
N D:CYS62 3.7 0.5 1.0
CB D:CYS62 3.8 0.2 1.0
N D:GLY63 3.9 0.2 1.0
N D:CYS78 4.1 92.1 1.0
N D:LYS64 4.2 91.7 1.0
CA D:CYS62 4.2 0.8 1.0
N D:TYR61 4.3 95.7 1.0
CA D:CYS75 4.3 80.2 1.0
CA D:CYS60 4.4 0.3 1.0
C D:CYS60 4.4 0.8 1.0
C D:CYS62 4.5 0.1 1.0
CA D:CYS78 4.5 86.0 1.0
CB D:LYS64 4.6 0.5 1.0
C D:TYR61 4.8 0.7 1.0
CA D:GLY63 4.8 0.7 1.0
CB D:ARG77 4.9 0.8 1.0
C D:GLY63 4.9 91.8 1.0
C D:CYS75 4.9 92.1 1.0
CA D:LYS64 4.9 0.8 1.0
CA D:TYR61 5.0 0.6 1.0

Reference:

J.Peek, M.Lilic, D.Montiel, A.Milshteyn, I.Woodworth, J.B.Biggins, M.A.Ternei, P.Y.Calle, M.Danziger, T.Warrier, K.Saito, N.Braffman, A.Fay, M.S.Glickman, S.A.Darst, E.A.Campbell, S.F.Brady. Rifamycin Congeners Kanglemycins Are Active Against Rifampicin-Resistant Bacteria Via A Distinct Mechanism. Nat Commun V. 9 4147 2018.
ISSN: ESSN 2041-1723
PubMed: 30297823
DOI: 10.1038/S41467-018-06587-2
Page generated: Mon Oct 28 18:41:30 2024

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