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Zinc in PDB 5nus: Structure of A Minimal Complex Between P44 and P34 From Chaetomium Thermophilum

Protein crystallography data

The structure of Structure of A Minimal Complex Between P44 and P34 From Chaetomium Thermophilum, PDB code: 5nus was solved by W.Koelmel, E.Schoenwetter, J.Kuper, D.R.Schmitt, C.Kisker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.42 / 2.20
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 147.056, 147.056, 87.599, 90.00, 90.00, 120.00
R / Rfree (%) 21 / 22.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of A Minimal Complex Between P44 and P34 From Chaetomium Thermophilum (pdb code 5nus). 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 A Minimal Complex Between P44 and P34 From Chaetomium Thermophilum, PDB code: 5nus:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5nus

Go back to Zinc Binding Sites List in 5nus
Zinc binding site 1 out of 2 in the Structure of A Minimal Complex Between P44 and P34 From Chaetomium Thermophilum


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of A Minimal Complex Between P44 and P34 From Chaetomium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn601

b:62.5
occ:1.00
SG B:CYS487 2.3 64.1 1.0
SG B:CYS404 2.3 75.4 1.0
SG B:CYS401 2.3 71.0 1.0
SG B:CYS484 2.6 66.6 1.0
H B:CYS404 2.9 69.0 1.0
HB3 B:CYS404 2.9 62.9 1.0
HB3 B:CYS401 3.0 74.9 1.0
CB B:CYS401 3.1 62.4 1.0
HB2 B:CYS487 3.1 72.3 1.0
H B:CYS484 3.1 80.0 1.0
HB2 B:CYS401 3.2 74.9 1.0
CB B:CYS404 3.2 52.4 1.0
HB3 B:CYS484 3.3 78.3 1.0
CB B:CYS487 3.3 60.3 1.0
CB B:CYS484 3.5 65.2 1.0
HB3 B:ALA403 3.6 65.3 1.0
N B:CYS404 3.6 57.5 1.0
HD3 A:LYS155 3.7 76.2 1.0
H B:CYS487 3.8 74.1 1.0
N B:CYS484 3.9 66.7 1.0
HB2 B:CYS404 4.0 62.9 1.0
CA B:CYS404 4.0 56.7 1.0
HB3 B:CYS487 4.0 72.3 1.0
HB3 B:ALA406 4.1 79.6 1.0
HZ1 A:LYS155 4.1 85.1 1.0
HE2 A:LYS155 4.2 81.2 1.0
H B:ALA406 4.3 80.8 1.0
CA B:CYS484 4.3 68.4 1.0
HB2 B:CYS484 4.3 78.3 1.0
N B:CYS487 4.3 61.7 1.0
H B:ALA403 4.4 73.9 1.0
CA B:CYS487 4.4 60.4 1.0
HB3 B:PHE483 4.5 80.3 1.0
CD A:LYS155 4.5 63.5 1.0
CB B:ALA403 4.5 54.4 1.0
HG2 A:LYS155 4.5 72.7 1.0
HB2 A:LYS155 4.6 68.9 1.0
CA B:CYS401 4.6 67.0 1.0
HB2 B:ASP486 4.6 81.9 1.0
H B:LEU405 4.7 77.4 1.0
CE A:LYS155 4.7 67.6 1.0
HA B:PHE483 4.7 81.5 1.0
C B:ALA403 4.7 56.2 1.0
C B:CYS404 4.7 60.7 1.0
HA B:CYS487 4.7 72.5 1.0
HA B:CYS404 4.7 68.1 1.0
HB2 B:ALA406 4.7 79.6 1.0
HD1 B:PHE483 4.8 74.5 1.0
O A:HOH307 4.8 56.5 1.0
NZ A:LYS155 4.8 70.9 1.0
CB B:ALA406 4.9 66.3 1.0
HB1 B:ALA403 4.9 65.3 1.0
C B:CYS484 4.9 70.6 1.0
N B:LEU405 4.9 64.5 1.0
HA B:CYS401 4.9 80.4 1.0
CG A:LYS155 5.0 60.6 1.0
N B:ALA403 5.0 61.6 1.0
CA B:ALA403 5.0 57.1 1.0

Zinc binding site 2 out of 2 in 5nus

Go back to Zinc Binding Sites List in 5nus
Zinc binding site 2 out of 2 in the Structure of A Minimal Complex Between P44 and P34 From Chaetomium Thermophilum


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of A Minimal Complex Between P44 and P34 From Chaetomium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn602

b:67.9
occ:1.00
SG B:CYS501 2.2 64.7 1.0
SG B:CYS479 2.2 81.9 1.0
SG B:CYS498 2.2 76.8 1.0
SG B:CYS476 2.4 80.3 1.0
H B:CYS501 2.8 80.4 1.0
HB3 B:CYS476 2.9 93.9 1.0
H B:CYS479 3.0 0.2 1.0
HB3 B:CYS479 3.0 90.9 1.0
CB B:CYS476 3.1 78.3 1.0
HB3 B:CYS498 3.2 80.8 1.0
CB B:CYS479 3.2 75.7 1.0
HB2 B:CYS476 3.2 93.9 1.0
CB B:CYS498 3.3 67.3 1.0
N B:CYS501 3.3 67.0 1.0
CB B:CYS501 3.4 69.1 1.0
HB2 B:CYS498 3.5 80.8 1.0
HB B:THR478 3.5 0.8 1.0
HB2 B:CYS501 3.6 82.9 1.0
N B:CYS479 3.7 86.8 1.0
HA3 B:GLY500 3.8 79.0 1.0
CA B:CYS501 3.9 67.4 1.0
HB2 B:CYS479 4.0 90.9 1.0
HA B:CYS501 4.0 80.8 1.0
CA B:CYS479 4.1 84.7 1.0
C B:GLY500 4.1 67.5 1.0
H B:GLY500 4.2 77.6 1.0
HB3 B:CYS501 4.3 82.9 1.0
CA B:GLY500 4.3 65.8 1.0
O B:HOH703 4.4 66.5 1.0
HE2 B:PHE483 4.4 80.6 1.0
HE1 B:TRP385 4.4 85.3 1.0
HZ B:PHE483 4.5 77.2 1.0
CB B:THR478 4.5 93.2 1.0
CA B:CYS476 4.6 81.7 1.0
H B:GLY480 4.6 0.3 1.0
N B:GLY500 4.6 64.7 1.0
H B:THR478 4.6 0.9 1.0
CA B:CYS498 4.6 65.3 1.0
HB2 B:LYS481 4.7 89.3 1.0
H B:LYS481 4.7 94.0 1.0
HA B:CYS479 4.8 0.7 1.0
C B:THR478 4.8 92.5 1.0
HZ2 B:TRP385 4.8 82.3 1.0
C B:CYS498 4.9 64.8 1.0
NE1 B:TRP385 4.9 71.1 1.0
C B:CYS479 4.9 85.1 1.0
C B:CYS476 5.0 87.0 1.0
HA B:CYS498 5.0 78.3 1.0

Reference:

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
Page generated: Wed Dec 16 06:36:37 2020

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