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Iron in PDB 5of4: The Cryo-Em Structure of Human Tfiih

Enzymatic activity of The Cryo-Em Structure of Human Tfiih

All present enzymatic activity of The Cryo-Em Structure of Human Tfiih:
3.6.4.12;

Iron Binding Sites:

The binding sites of Iron atom in the The Cryo-Em Structure of Human Tfiih (pdb code 5of4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the The Cryo-Em Structure of Human Tfiih, PDB code: 5of4:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 5of4

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Iron binding site 1 out of 4 in the The Cryo-Em Structure of Human Tfiih


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Cryo-Em Structure of Human Tfiih within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1000

b:97.0
occ:1.00
FE1 B:SF41000 0.0 97.0 1.0
S4 B:SF41000 2.1 0.6 1.0
S2 B:SF41000 2.1 95.2 1.0
S3 B:SF41000 2.2 0.7 1.0
SG B:CYS116 2.2 0.2 1.0
FE3 B:SF41000 2.9 0.4 1.0
FE2 B:SF41000 2.9 0.3 1.0
CB B:CYS116 3.0 0.5 1.0
FE4 B:SF41000 3.3 0.8 1.0
CA B:CYS116 3.6 0.6 1.0
CD2 B:HIS118 3.7 0.2 1.0
S1 B:SF41000 3.8 0.6 1.0
SG B:CYS134 4.2 0.2 1.0
NE2 B:HIS118 4.3 0.9 1.0
N B:ILE117 4.5 1.0 1.0
C B:CYS116 4.6 0.5 1.0
N B:CYS116 4.6 0.9 1.0
CG B:HIS118 4.7 0.3 1.0
O B:LEU115 4.7 0.4 1.0
CB B:CYS134 4.8 0.2 1.0
C B:LEU115 5.0 0.8 1.0
CG1 B:VAL121 5.0 0.2 1.0

Iron binding site 2 out of 4 in 5of4

Go back to Iron Binding Sites List in 5of4
Iron binding site 2 out of 4 in the The Cryo-Em Structure of Human Tfiih


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Cryo-Em Structure of Human Tfiih within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1000

b:0.3
occ:1.00
FE2 B:SF41000 0.0 0.3 1.0
S3 B:SF41000 2.1 0.7 1.0
S4 B:SF41000 2.2 0.6 1.0
S1 B:SF41000 2.2 0.6 1.0
SG B:CYS155 2.3 0.7 1.0
FE1 B:SF41000 2.9 97.0 1.0
FE4 B:SF41000 3.0 0.8 1.0
FE3 B:SF41000 3.0 0.4 1.0
S2 B:SF41000 3.6 95.2 1.0
CB B:CYS155 3.8 0.1 1.0
OG1 B:THR138 3.9 0.2 1.0
NE2 B:HIS118 4.2 0.9 1.0
SG B:CYS134 4.2 0.2 1.0
CD2 B:HIS118 4.3 0.2 1.0
CA B:CYS155 4.5 0.6 1.0
SG B:CYS190 4.7 0.1 1.0
SG B:CYS116 4.9 0.2 1.0

Iron binding site 3 out of 4 in 5of4

Go back to Iron Binding Sites List in 5of4
Iron binding site 3 out of 4 in the The Cryo-Em Structure of Human Tfiih


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Cryo-Em Structure of Human Tfiih within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1000

b:0.4
occ:1.00
FE3 B:SF41000 0.0 0.4 1.0
S1 B:SF41000 2.1 0.6 1.0
S4 B:SF41000 2.2 0.6 1.0
S2 B:SF41000 2.3 95.2 1.0
SG B:CYS134 2.3 0.2 1.0
FE1 B:SF41000 2.9 97.0 1.0
FE4 B:SF41000 2.9 0.8 1.0
FE2 B:SF41000 3.0 0.3 1.0
S3 B:SF41000 3.6 0.7 1.0
CB B:CYS134 3.8 0.2 1.0
CD1 B:LEU115 4.2 0.6 1.0
CG B:LEU115 4.3 0.8 1.0
CD2 B:LEU115 4.7 93.3 1.0
CE2 B:PHE193 4.8 0.5 1.0
OG1 B:THR138 4.8 0.2 1.0
SG B:CYS116 4.9 0.2 1.0
CA B:CYS134 4.9 0.5 1.0
SG B:CYS190 5.0 0.1 1.0
CB B:CYS116 5.0 0.5 1.0

Iron binding site 4 out of 4 in 5of4

Go back to Iron Binding Sites List in 5of4
Iron binding site 4 out of 4 in the The Cryo-Em Structure of Human Tfiih


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The Cryo-Em Structure of Human Tfiih within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1000

b:0.8
occ:1.00
FE4 B:SF41000 0.0 0.8 1.0
S2 B:SF41000 2.1 95.2 1.0
S1 B:SF41000 2.1 0.6 1.0
SG B:CYS190 2.2 0.1 1.0
S3 B:SF41000 2.2 0.7 1.0
FE3 B:SF41000 2.9 0.4 1.0
FE2 B:SF41000 3.0 0.3 1.0
FE1 B:SF41000 3.3 97.0 1.0
CB B:CYS190 3.6 96.4 1.0
S4 B:SF41000 3.8 0.6 1.0
CE2 B:PHE157 4.1 0.4 1.0
CA B:CYS190 4.4 0.1 1.0
O B:LEU115 4.5 0.4 1.0
CE2 B:PHE193 4.5 0.5 1.0
CD2 B:PHE157 4.6 0.5 1.0
CD2 B:PHE193 4.7 0.5 1.0
SG B:CYS155 4.8 0.7 1.0
CZ B:PHE157 4.9 0.9 1.0
CD1 B:LEU115 4.9 0.6 1.0

Reference:

B.J.Greber, T.H.D.Nguyen, J.Fang, P.V.Afonine, P.D.Adams, E.Nogales. The Cryo-Electron Microscopy Structure of Human Transcription Factor Iih. Nature V. 549 414 2017.
ISSN: ESSN 1476-4687
PubMed: 28902838
DOI: 10.1038/NATURE23903
Page generated: Tue Aug 6 06:57:06 2024

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