Zinc in PDB 5o85: P34-P44 Complex

The structure of P34-P44 Complex, PDB code: 5o85 was solved by L.Radu, A.Poterszman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.70 / 3.40
Space group	I 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	81.407, 120.388, 128.673, 90.00, 90.00, 90.00
R / Rfree (%)	24 / 29

The binding sites of Zinc atom in the P34-P44 Complex (pdb code 5o85). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the P34-P44 Complex, PDB code: 5o85:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the P34-P44 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of P34-P44 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:0.2 occ:1.00 SG B:CYS368 2.4 0.5 1.0 SG B:CYS371 2.5 0.7 1.0 SG B:CYS348 2.5 0.8 1.0 SG B:CYS345 2.7 0.1 1.0 CB B:CYS345 3.2 0.4 1.0 CB B:CYS368 3.4 0.8 1.0 CB B:CYS371 3.4 0.9 1.0 N B:CYS348 3.6 0.6 1.0 CB B:CYS348 3.7 0.3 1.0 N B:CYS368 3.8 0.0 1.0 CA B:CYS368 4.1 0.1 1.0 CA B:CYS348 4.2 0.2 1.0 N B:CYS371 4.4 0.1 1.0 CA B:CYS371 4.5 0.3 1.0 CA B:CYS345 4.7 0.9 1.0 C B:GLY347 4.7 0.9 1.0 C B:CYS368 4.7 0.6 1.0 CA B:GLY347 4.8 0.6 1.0 N B:GLY347 4.8 0.7 1.0 N B:GLN349 4.8 0.3 1.0 C B:CYS348 4.9 0.6 1.0 O B:CYS368 4.9 0.7 1.0 O B:GLY350 4.9 0.8 1.0 C B:PHE367 4.9 0.5 1.0 N B:GLY350 5.0 0.7 1.0

Zinc binding site 2 out of 4 in the P34-P44 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of P34-P44 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:0.4 occ:1.00 SG B:CYS360 2.5 0.7 1.0 SG B:CYS382 2.5 0.7 1.0 SG B:CYS385 2.6 0.3 1.0 SG B:CYS363 2.6 0.2 1.0 CB B:CYS360 3.1 0.3 1.0 CB B:CYS382 3.3 0.7 1.0 N B:CYS385 3.6 0.6 1.0 CB B:CYS363 3.8 0.8 1.0 CB B:CYS385 3.9 0.2 1.0 CA B:CYS385 4.1 0.8 1.0 N B:CYS363 4.2 0.5 1.0 C B:GLY384 4.2 0.7 1.0 CA B:GLY384 4.5 0.6 1.0 CA B:CYS363 4.6 0.1 1.0 CE1 B:PHE331 4.6 0.8 1.0 CA B:CYS360 4.6 0.9 1.0 N B:GLY384 4.7 0.5 1.0 CA B:CYS382 4.7 0.0 1.0 CB B:VAL362 4.8 0.5 1.0 CE2 B:PHE367 4.9 0.1 1.0

Zinc binding site 3 out of 4 in the P34-P44 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of P34-P44 Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn401 b:0.2 occ:1.00 SG D:CYS371 2.4 0.2 1.0 SG D:CYS345 2.4 0.4 1.0 SG D:CYS368 2.5 0.7 1.0 CB D:CYS371 2.8 0.1 1.0 SG D:CYS348 2.9 0.3 1.0 CB D:CYS345 3.3 0.3 1.0 CB D:CYS368 3.4 0.9 1.0 N D:CYS368 3.5 0.5 1.0 N D:CYS348 3.9 1.0 1.0 CB D:CYS348 3.9 0.9 1.0 CA D:CYS368 4.0 0.0 1.0 CA D:CYS371 4.0 1.0 1.0 N D:CYS371 4.0 0.0 1.0 CA D:CYS348 4.5 0.9 1.0 C D:PHE367 4.5 0.6 1.0 C D:CYS368 4.6 0.8 1.0 CA D:PHE367 4.7 0.5 1.0 O D:CYS368 4.7 0.5 1.0 CA D:GLY347 4.8 0.5 1.0 N D:GLY347 4.8 0.8 1.0 CA D:CYS345 4.8 0.8 1.0 C D:GLY347 4.8 0.6 1.0 CB D:PHE367 4.9 0.4 1.0 C D:CYS371 5.0 0.0 1.0

Zinc binding site 4 out of 4 in the P34-P44 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of P34-P44 Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn402 b:0.4 occ:1.00 SG D:CYS385 2.4 0.6 1.0 SG D:CYS363 2.5 0.4 1.0 SG D:CYS382 2.7 0.2 1.0 SG D:CYS360 2.7 0.4 1.0 CB D:CYS363 3.4 0.0 1.0 CB D:CYS360 3.5 0.6 1.0 N D:CYS385 3.5 0.2 1.0 CB D:CYS382 3.5 0.9 1.0 CB D:CYS385 3.7 0.8 1.0 N D:CYS363 3.7 0.2 1.0 CA D:CYS385 3.9 0.4 1.0 C D:GLY384 4.1 0.3 1.0 CA D:CYS363 4.2 0.1 1.0 CB D:VAL362 4.3 0.1 1.0 CA D:GLY384 4.5 1.0 1.0 C D:VAL362 4.7 0.4 1.0 N D:GLY384 4.8 0.9 1.0 N D:VAL362 4.8 0.9 1.0 CA D:VAL362 4.8 0.8 1.0 O D:GLY384 4.8 1.0 1.0 CG2 D:VAL362 4.9 0.3 1.0 CA D:CYS360 4.9 0.2 1.0 CA D:CYS382 5.0 0.6 1.0 C D:CYS363 5.0 0.9 1.0

L.Radu, E.Schoenwetter, C.Braun, J.Marcoux, W.Koelmel, D.R.Schmitt, J.Kuper, S.Cianferani, J.M.Egly, A.Poterszman, C.Kisker. The Intricate Network Between the P34 and P44 Subunits Is Central to the Activity of the Transcription/Dna Repair Factor Tfiih. Nucleic Acids Res. V. 45 10872 2017.
ISSN: ESSN 1362-4962
PubMed: 28977422
DOI: 10.1093/NAR/GKX743