Zinc in PDB 3wod: Rna Polymerase-GP39 Complex

All present enzymatic activity of Rna Polymerase-GP39 Complex:
2.7.7.6;

The structure of Rna Polymerase-GP39 Complex, PDB code: 3wod was solved by S.Tagami, S.Sekine, L.Minakhin, D.Esyunina, R.Akasaka, M.Shirouzu, A.Kulbachinskiy, K.Severinov, S.Yokoyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.88 / 3.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	294.442, 294.442, 223.255, 90.00, 90.00, 120.00
R / Rfree (%)	25 / 27.9

The binding sites of Zinc atom in the Rna Polymerase-GP39 Complex (pdb code 3wod). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Rna Polymerase-GP39 Complex, PDB code: 3wod:

Zinc binding site 1 out of 1 in the Rna Polymerase-GP39 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Rna Polymerase-GP39 Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1601 b:0.5 occ:1.00 SG D:CYS1204 2.1 0.1 1.0 SG D:CYS1201 2.2 75.7 1.0 SG D:CYS1112 2.2 55.0 1.0 CA D:CYS1194 2.6 97.5 1.0 CB D:CYS1194 2.7 0.0 1.0 CB D:CYS1204 2.9 0.5 1.0 SG D:CYS1194 3.3 0.9 1.0 N D:GLN1195 3.4 0.4 1.0 C D:CYS1194 3.5 0.3 1.0 N D:CYS1194 3.8 79.8 1.0 NH1 D:ARG1189 3.8 0.2 1.0 CG2 D:THR1114 3.8 72.9 1.0 CB D:CYS1201 3.9 68.6 1.0 CB D:CYS1112 4.0 69.2 1.0 O D:THR1193 4.0 0.5 1.0 CA D:CYS1204 4.2 93.8 1.0 C D:THR1193 4.3 95.0 1.0 O D:SER1190 4.3 92.0 1.0 N D:CYS1201 4.4 72.6 1.0 N D:CYS1204 4.6 92.6 1.0 O D:CYS1194 4.7 82.9 1.0 CG1 D:VAL1200 4.7 32.9 1.0 CA D:CYS1201 4.7 73.8 1.0 CA D:GLN1195 4.7 0.8 1.0 O D:CYS1112 4.7 94.6 1.0 OG1 D:THR1196 4.9 0.4 1.0 CZ D:ARG1189 4.9 0.5 1.0 CA D:CYS1112 5.0 71.5 1.0

S.Tagami, S.Sekine, L.Minakhin, D.Esyunina, R.Akasaka, M.Shirouzu, A.Kulbachinskiy, K.Severinov, S.Yokoyama. Structural Basis For Promoter Specificity Switching of Rna Polymerase By A Phage Factor Genes Dev. V. 28 521 2014.
ISSN: ISSN 0890-9369
DOI: 10.1101/GAD.233916.113