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Zinc in PDB 2e2j: Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp

Enzymatic activity of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp

All present enzymatic activity of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp:
2.7.7.6;

Protein crystallography data

The structure of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp, PDB code: 2e2j was solved by D.Wang, D.A.Bushnell, K.D.Westover, C.D.Kaplan, R.D.Kornberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 3.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 170.142, 222.017, 194.652, 90.00, 101.36, 90.00
R / Rfree (%) 24.2 / 30.6

Other elements in 2e2j:

The structure of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp (pdb code 2e2j). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp, PDB code: 2e2j:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Zinc binding site 1 out of 8 in 2e2j

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Zinc binding site 1 out of 8 in the Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1734

b:0.3
occ:1.00
 SG A:CYS107 2.4 0.2 1.0
SG A:CYS148 2.4 0.6 1.0
SG A:CYS110 2.4 0.3 1.0
SG A:CYS167 2.4 0.6 1.0
CB A:CYS107 3.4 0.8 1.0
CB A:CYS167 3.5 0.1 1.0
CB A:CYS110 3.5 0.4 1.0
CB A:CYS148 3.5 0.8 1.0
N A:CYS167 3.7 0.2 1.0
O A:MET108 3.7 0.2 1.0
CA A:CYS167 4.1 0.2 1.0
N A:CYS110 4.4 0.2 1.0
CA A:CYS110 4.5 0.2 1.0
N A:GLY168 4.5 0.9 1.0
C A:GLY166 4.6 0.2 1.0
CA A:CYS148 4.7 1.0 1.0
C A:CYS167 4.8 0.0 1.0
CA A:CYS107 4.8 0.4 1.0
N A:GLY111 4.8 0.4 1.0
CA A:GLY166 4.8 0.3 1.0
C A:MET108 4.9 0.2 1.0
N A:MET108 5.0 0.8 1.0
C A:CYS107 5.0 0.6 1.0

Zinc binding site 2 out of 8 in 2e2j

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Zinc binding site 2 out of 8 in the Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1735

b:0.8
occ:1.00
 NE2 A:HIS80 1.8 0.3 1.0
SG A:CYS77 2.3 0.1 1.0
SG A:CYS70 2.3 1.0 1.0
SG A:CYS67 2.3 0.0 1.0
CE1 A:HIS80 2.5 0.6 1.0
CD2 A:HIS80 3.0 0.8 1.0
CB A:CYS77 3.4 0.5 1.0
CB A:CYS70 3.4 0.1 1.0
CB A:CYS67 3.5 0.5 1.0
ND1 A:HIS80 3.7 0.5 1.0
O A:CYS67 3.7 0.7 1.0
NE2 A:GLN68 3.9 0.6 1.0
CG A:HIS80 4.0 0.2 1.0
CA A:CYS77 4.3 0.1 1.0
C A:CYS67 4.6 0.8 1.0
CA A:CYS67 4.6 0.8 1.0
O A:GLN71 4.7 0.5 1.0
CD A:PRO78 4.8 0.0 1.0
CA A:CYS70 4.8 0.5 1.0
C A:CYS70 5.0 0.2 1.0

Zinc binding site 3 out of 8 in 2e2j

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Zinc binding site 3 out of 8 in the Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1307

b:0.8
occ:1.00
 SG B:CYS1163 2.3 0.6 1.0
SG B:CYS1166 2.3 0.1 1.0
SG B:CYS1185 2.3 0.3 1.0
SG B:CYS1182 2.4 0.1 1.0
CB B:CYS1163 3.3 0.4 1.0
CB B:CYS1185 3.3 0.2 1.0
CB B:CYS1182 3.5 0.8 1.0
CB B:CYS1166 3.5 0.1 1.0
N B:CYS1166 3.7 0.2 1.0
O B:CYS1166 4.0 0.1 1.0
CA B:CYS1166 4.0 0.1 1.0
C B:CYS1166 4.5 0.9 1.0
CB B:ILE1165 4.6 0.6 1.0
CA B:CYS1163 4.7 0.1 1.0
CA B:CYS1185 4.8 0.4 1.0
C B:ILE1165 4.8 0.3 1.0
CA B:CYS1182 4.9 0.2 1.0
OG1 B:THR1170 4.9 0.3 1.0
CB B:ASN1187 5.0 0.8 1.0

Zinc binding site 4 out of 8 in 2e2j

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Zinc binding site 4 out of 8 in the Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn319

b:90.4
occ:1.00
 SG C:CYS86 2.3 89.3 1.0
SG C:CYS92 2.3 91.9 1.0
SG C:CYS88 2.3 86.8 1.0
SG C:CYS95 2.3 86.3 1.0
N C:CYS92 3.1 93.0 1.0
CB C:CYS95 3.3 84.3 1.0
CB C:CYS92 3.3 92.7 1.0
CB C:CYS88 3.4 88.2 1.0
CB C:CYS86 3.4 89.5 1.0
CA C:CYS92 3.7 92.7 1.0
C C:HIS91 4.0 93.5 1.0
N C:CYS95 4.0 85.5 1.0
CA C:CYS95 4.3 83.8 1.0
CA C:HIS91 4.3 93.7 1.0
C C:CYS92 4.3 92.7 1.0
O C:CYS92 4.5 93.0 1.0
CA C:CYS88 4.5 88.5 1.0
N C:CYS88 4.5 87.9 1.0
CA C:CYS86 4.8 89.5 1.0
C C:LYS94 4.9 87.3 1.0
CB C:LYS94 4.9 89.2 1.0
C C:CYS86 5.0 89.1 1.0
N C:LYS94 5.0 89.3 1.0

Zinc binding site 5 out of 8 in 2e2j

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Zinc binding site 5 out of 8 in the Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Zn203

b:0.9
occ:1.00
 SG I:CYS10 2.3 0.9 1.0
SG I:CYS29 2.3 0.6 1.0
SG I:CYS32 2.4 0.8 1.0
SG I:CYS7 2.4 0.3 1.0
N I:CYS32 3.3 99.6 1.0
CB I:CYS10 3.3 0.7 1.0
CB I:THR31 3.4 0.6 1.0
CB I:CYS7 3.4 0.5 1.0
CB I:CYS32 3.6 99.3 1.0
CB I:CYS29 3.6 99.7 1.0
CA I:CYS32 4.0 99.1 1.0
OG1 I:THR31 4.1 0.8 1.0
C I:THR31 4.2 0.2 1.0
CA I:THR31 4.2 0.5 1.0
CG2 I:THR31 4.2 1.0 1.0
N I:THR31 4.4 0.4 1.0
N I:CYS10 4.4 0.6 1.0
CA I:CYS10 4.4 0.1 1.0
CB I:ASN12 4.6 0.4 1.0
C I:CYS32 4.8 98.4 1.0
CA I:CYS7 4.8 0.1 1.0
CB I:TYR34 4.9 94.2 1.0
O I:CYS7 4.9 0.1 1.0
CA I:CYS29 5.0 99.5 1.0

Zinc binding site 6 out of 8 in 2e2j

Go back to Zinc Binding Sites List in 2e2j
Zinc binding site 6 out of 8 in the Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Zn204

b:90.2
occ:1.00
 SG I:CYS106 2.3 89.2 1.0
SG I:CYS75 2.3 94.8 1.0
SG I:CYS78 2.3 94.3 1.0
SG I:CYS103 2.4 85.0 1.0
O I:CYS78 3.2 95.8 1.0
CB I:CYS75 3.3 95.4 1.0
CB I:CYS103 3.4 85.7 1.0
CB I:CYS106 3.4 89.4 1.0
CB I:CYS78 3.5 95.3 1.0
N I:CYS78 3.5 95.8 1.0
CA I:CYS78 3.8 95.5 1.0
C I:CYS78 3.9 95.6 1.0
N I:CYS106 4.1 89.4 1.0
OG I:SER80 4.3 94.4 1.0
CB I:LYS77 4.4 96.3 1.0
CA I:CYS106 4.4 89.4 1.0
CB I:HIS108 4.5 87.3 1.0
C I:LYS77 4.6 95.8 1.0
CA I:CYS75 4.7 95.7 1.0
C I:SER105 4.8 89.4 1.0
CA I:CYS103 4.8 85.4 1.0
CB I:SER105 4.9 89.5 1.0
CA I:LYS77 4.9 95.9 1.0

Zinc binding site 7 out of 8 in 2e2j

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Zinc binding site 7 out of 8 in the Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn101

b:77.2
occ:1.00
 SG J:CYS45 2.3 74.9 1.0
SG J:CYS10 2.3 77.5 1.0
SG J:CYS7 2.3 79.0 1.0
SG J:CYS46 2.3 71.8 1.0
N J:CYS46 2.9 73.9 1.0
C J:CYS45 3.3 74.5 1.0
CB J:CYS45 3.3 75.4 1.0
CB J:CYS10 3.3 78.0 1.0
CA J:CYS46 3.3 73.4 1.0
CB J:CYS46 3.4 73.1 1.0
N J:CYS10 3.4 77.7 1.0
CB J:CYS7 3.6 77.4 1.0
O J:CYS45 3.8 74.3 1.0
CA J:CYS45 3.9 75.1 1.0
CA J:CYS10 3.9 77.8 1.0
CD J:ARG43 4.1 86.1 1.0
CG J:ARG43 4.1 86.0 1.0
OG J:SER9 4.2 77.4 1.0
C J:SER9 4.2 77.7 1.0
N J:CYS45 4.6 76.5 1.0
N J:SER9 4.6 78.0 1.0
CA J:SER9 4.6 77.7 1.0
CB J:SER9 4.6 77.4 1.0
C J:CYS46 4.8 73.2 1.0
CA J:CYS7 4.9 77.5 1.0
N J:GLY11 4.9 78.6 1.0
C J:CYS10 5.0 78.0 1.0

Zinc binding site 8 out of 8 in 2e2j

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Zinc binding site 8 out of 8 in the Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Rna Polymerase II Elongation Complex in 5 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Zn105

b:0.2
occ:1.00
 SG L:CYS51 2.3 0.1 1.0
SG L:CYS34 2.3 0.7 1.0
SG L:CYS48 2.4 0.5 1.0
SG L:CYS31 2.4 0.5 1.0
CB L:CYS48 3.4 1.0 1.0
CB L:CYS51 3.4 0.6 1.0
CB L:CYS31 3.4 0.4 1.0
CB L:CYS34 3.5 0.7 1.0
N L:CYS34 4.1 0.6 1.0
CA L:CYS34 4.3 0.8 1.0
CB L:SER36 4.8 0.7 1.0
CA L:CYS51 4.8 0.4 1.0
CA L:CYS48 4.8 0.1 1.0
CA L:CYS31 4.9 0.4 1.0
C L:CYS34 4.9 0.0 1.0

Reference:

D.Wang, D.A.Bushnell, K.D.Westover, C.D.Kaplan, R.D.Kornberg. Structural Basis of Transcription: Role of the Trigger Loop in Substrate Specificity and Catalysis Cell(Cambridge,Mass.) V. 127 941 2006.
ISSN: ISSN 0092-8674
PubMed: 17129781
DOI: 10.1016/J.CELL.2006.11.023
Page generated: Wed Oct 16 22:58:31 2024

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