Zinc in PDB 6yys: Structure of Mycobacterium Smegmatis Held Protein in Complex with Rna Polymerase Core - State II, Primary Channel Engaged and Active Site Interfering

Enzymatic activity of Structure of Mycobacterium Smegmatis Held Protein in Complex with Rna Polymerase Core - State II, Primary Channel Engaged and Active Site Interfering

All present enzymatic activity of Structure of Mycobacterium Smegmatis Held Protein in Complex with Rna Polymerase Core - State II, Primary Channel Engaged and Active Site Interfering:
2.7.7.6; 3.6.4.12;

Other elements in 6yys:

The structure of Structure of Mycobacterium Smegmatis Held Protein in Complex with Rna Polymerase Core - State II, Primary Channel Engaged and Active Site Interfering also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Mycobacterium Smegmatis Held Protein in Complex with Rna Polymerase Core - State II, Primary Channel Engaged and Active Site Interfering (pdb code 6yys). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Mycobacterium Smegmatis Held Protein in Complex with Rna Polymerase Core - State II, Primary Channel Engaged and Active Site Interfering, PDB code: 6yys:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6yys

Go back to Zinc Binding Sites List in 6yys
Zinc binding site 1 out of 2 in the Structure of Mycobacterium Smegmatis Held Protein in Complex with Rna Polymerase Core - State II, Primary Channel Engaged and Active Site Interfering


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Mycobacterium Smegmatis Held Protein in Complex with Rna Polymerase Core - State II, Primary Channel Engaged and Active Site Interfering within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn2001

b:41.8
occ:1.00
 SG D:CYS974 2.2 16.2 1.0
SG D:CYS977 2.2 15.0 1.0
SG D:CYS890 2.3 20.2 1.0
SG D:CYS967 2.3 17.6 1.0
CB D:CYS977 2.9 15.0 1.0
CB D:CYS890 3.0 20.2 1.0
CB D:CYS967 3.1 17.6 1.0
CB D:CYS974 3.2 16.2 1.0
CA D:CYS967 3.6 17.6 1.0
NH2 D:ARG962 3.9 19.5 1.0
N D:CYS890 3.9 20.2 1.0
CA D:CYS977 4.1 15.0 1.0
CA D:CYS890 4.1 20.2 1.0
N D:CYS977 4.1 15.0 1.0
N D:CYS974 4.1 16.2 1.0
CA D:CYS974 4.2 16.2 1.0
OG D:SER969 4.4 18.1 1.0
C D:CYS967 4.5 17.6 1.0
N D:THR968 4.6 18.5 1.0
O D:CYS974 4.6 16.2 1.0
N D:CYS967 4.7 17.6 1.0
C D:CYS974 4.7 16.2 1.0
CZ D:ARG962 4.8 19.5 1.0
CG2 D:THR892 4.9 22.5 1.0
NE D:ARG962 5.0 19.5 1.0

Zinc binding site 2 out of 2 in 6yys

Go back to Zinc Binding Sites List in 6yys
Zinc binding site 2 out of 2 in the Structure of Mycobacterium Smegmatis Held Protein in Complex with Rna Polymerase Core - State II, Primary Channel Engaged and Active Site Interfering


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Mycobacterium Smegmatis Held Protein in Complex with Rna Polymerase Core - State II, Primary Channel Engaged and Active Site Interfering within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn2002

b:92.3
occ:1.00
 CB D:CYS62 2.1 72.5 1.0
SG D:CYS78 2.5 72.8 1.0
SG D:CYS75 2.5 69.7 1.0
SG D:CYS60 2.5 71.6 1.0
SG D:CYS62 2.8 72.5 1.0
CA D:CYS62 3.3 72.5 1.0
CB D:CYS78 3.4 72.8 1.0
N D:CYS62 3.4 72.5 1.0
CB D:LYS64 3.9 72.0 1.0
CB D:CYS75 3.9 69.7 1.0
N D:CYS78 3.9 72.8 1.0
CB D:CYS60 4.0 71.6 1.0
C D:CYS62 4.0 72.5 1.0
CB D:ARG77 4.2 73.0 1.0
N D:LYS64 4.3 72.0 1.0
CA D:CYS78 4.3 72.8 1.0
N D:GLY63 4.3 68.3 1.0
CG D:ARG77 4.4 73.0 1.0
CD D:ARG77 4.6 73.0 1.0
C D:TYR61 4.6 73.1 1.0
CD D:LYS64 4.7 72.0 1.0
O D:CYS62 4.7 72.5 1.0
CA D:LYS64 4.7 72.0 1.0
C D:ARG77 4.8 73.0 1.0
N D:TYR61 4.8 73.1 1.0
CG D:LYS64 4.9 72.0 1.0
CA D:ARG77 4.9 73.0 1.0
C D:CYS60 5.0 71.6 1.0

Reference:

T.Kouba, T.Koval, J.Dohnalek, L.Krasny. Held, A Helicase-Like Protein From Gram-Positive Bacteria in Complex with Rna Polymerase (State 2) To Be Published.
Page generated: Wed Dec 16 13:19:18 2020

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