Zinc in PDB 6o9m: Structure of the Human Apo Tfiih

Enzymatic activity of Structure of the Human Apo Tfiih

All present enzymatic activity of Structure of the Human Apo Tfiih:
3.6.4.12;

Other elements in 6o9m:

The structure of Structure of the Human Apo Tfiih also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Human Apo Tfiih (pdb code 6o9m). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Structure of the Human Apo Tfiih, PDB code: 6o9m:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 6o9m

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Zinc binding site 1 out of 6 in the Structure of the Human Apo Tfiih


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Human Apo Tfiih within 5.0Å range:
probe atom residue distance (Å) B Occ
3:Zn401

b:0.0
occ:1.00
 SG 3:CYS31 2.5 0.0 1.0
SG 3:CYS6 2.5 0.0 1.0
SG 3:CYS34 2.5 0.0 1.0
OG1 3:THR12 3.2 0.0 1.0
O 3:CYS9 3.4 0.0 1.0
CB 3:CYS6 3.6 0.0 1.0
CB 3:CYS34 4.0 0.0 1.0
CB 3:CYS31 4.0 0.0 1.0
CB 3:THR12 4.0 0.0 1.0
CB 3:ARG8 4.2 0.0 1.0
N 3:CYS34 4.2 0.0 1.0
C 3:CYS9 4.6 0.0 1.0
CA 3:CYS34 4.6 0.0 1.0
CB 3:SER33 4.7 0.0 1.0
SG 3:CYS9 4.7 0.0 1.0
N 3:CYS9 4.8 0.0 1.0
C 3:SER33 4.8 0.0 1.0
CG2 3:THR12 4.8 0.0 1.0
C 3:ARG8 4.9 0.0 1.0
CA 3:CYS6 4.9 0.0 1.0

Zinc binding site 2 out of 6 in 6o9m

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Zinc binding site 2 out of 6 in the Structure of the Human Apo Tfiih


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Human Apo Tfiih within 5.0Å range:
probe atom residue distance (Å) B Occ
3:Zn402

b:0.0
occ:1.00
 CB 3:CYS26 2.6 0.0 1.0
SG 3:CYS26 2.8 0.0 1.0
CG2 3:THR51 3.4 0.0 1.0
CA 3:CYS26 4.0 0.0 1.0
CB 3:THR51 4.2 0.0 1.0
OG1 3:THR51 4.2 0.0 1.0
N 3:CYS26 4.4 0.0 1.0
CG1 3:VAL25 4.7 0.0 1.0

Zinc binding site 3 out of 6 in 6o9m

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Zinc binding site 3 out of 6 in the Structure of the Human Apo Tfiih


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of the Human Apo Tfiih within 5.0Å range:
probe atom residue distance (Å) B Occ
4:Zn401

b:0.0
occ:1.00
 OG 4:SER273 2.1 0.0 1.0
N 4:SER269 2.2 0.0 1.0
SG 4:CYS271 2.4 0.0 1.0
CB 4:SER269 2.5 0.0 1.0
CG2 4:THR284 2.5 0.0 1.0
CA 4:SER269 2.7 0.0 1.0
OG 4:SER269 2.9 0.0 1.0
C 4:CYS268 3.0 0.0 1.0
OG1 4:THR284 3.1 0.0 1.0
CB 4:THR284 3.1 0.0 1.0
CB 4:CYS268 3.4 0.0 1.0
CB 4:SER273 3.4 0.0 1.0
C 4:SER269 3.4 0.0 1.0
CA 4:CYS268 3.6 0.0 1.0
O 4:SER269 3.7 0.0 1.0
OE1 1:GLN355 3.8 0.0 1.0
O 4:CYS268 3.8 0.0 1.0
SG 4:CYS268 4.0 0.0 1.0
N 4:CYS268 4.1 0.0 1.0
CB 4:CYS271 4.1 0.0 1.0
N 4:SER273 4.3 0.0 1.0
O 4:SER273 4.3 0.0 1.0
N 4:VAL270 4.3 0.0 1.0
CA 4:SER273 4.4 0.0 1.0
CD 1:GLN355 4.5 0.0 1.0
N 4:CYS271 4.5 0.0 1.0
CA 4:THR284 4.6 0.0 1.0
NE2 1:GLN355 4.6 0.0 1.0
CA 4:CYS271 4.8 0.0 1.0
C 4:SER273 4.9 0.0 1.0

Zinc binding site 4 out of 6 in 6o9m

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Zinc binding site 4 out of 6 in the Structure of the Human Apo Tfiih


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of the Human Apo Tfiih within 5.0Å range:
probe atom residue distance (Å) B Occ
6:Zn401

b:0.0
occ:1.00
 N 6:CYS368 2.2 0.0 1.0
SG 6:CYS371 2.5 0.0 1.0
SG 6:CYS345 2.5 0.0 1.0
SG 6:CYS368 2.5 0.0 1.0
CB 6:CYS371 2.5 0.0 1.0
CB 6:CYS368 2.9 0.0 1.0
CA 6:CYS368 3.0 0.0 1.0
C 6:PHE367 3.1 0.0 1.0
CA 6:PHE367 3.3 0.0 1.0
CB 6:CYS345 3.6 0.0 1.0
CB 6:PHE367 3.7 0.0 1.0
CA 6:CYS371 3.7 0.0 1.0
N 6:CYS371 3.7 0.0 1.0
C 6:CYS368 3.8 0.0 1.0
SG 6:CYS348 3.9 0.0 1.0
O 6:CYS368 3.9 0.0 1.0
O 6:PHE367 4.2 0.0 1.0
CD1 6:PHE367 4.3 0.0 1.0
CG 6:PHE367 4.5 0.0 1.0
N 6:CYS348 4.6 0.0 1.0
N 6:PHE367 4.6 0.0 1.0
O 6:VAL366 4.7 0.0 1.0
C 6:CYS371 4.7 0.0 1.0
C 6:ASP370 4.8 0.0 1.0
CA 6:CYS345 4.9 0.0 1.0
N 6:VAL369 4.9 0.0 1.0
CB 6:CYS348 4.9 0.0 1.0
N 6:GLY347 5.0 0.0 1.0

Zinc binding site 5 out of 6 in 6o9m

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Zinc binding site 5 out of 6 in the Structure of the Human Apo Tfiih


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Structure of the Human Apo Tfiih within 5.0Å range:
probe atom residue distance (Å) B Occ
6:Zn402

b:0.0
occ:1.00
 N 6:CYS385 2.1 0.0 1.0
SG 6:CYS382 2.4 0.0 1.0
SG 6:CYS363 2.5 0.0 1.0
SG 6:CYS385 2.6 0.0 1.0
C 6:GLY384 2.7 0.0 1.0
CB 6:CYS382 3.0 0.0 1.0
CA 6:GLY384 3.0 0.0 1.0
CA 6:CYS385 3.1 0.0 1.0
N 6:GLY384 3.3 0.0 1.0
CB 6:CYS385 3.3 0.0 1.0
O 6:CYS382 3.5 0.0 1.0
O 6:GLY384 3.5 0.0 1.0
CB 6:CYS363 3.7 0.0 1.0
C 6:CYS382 3.8 0.0 1.0
SG 6:CYS360 3.8 0.0 1.0
CA 6:CYS382 4.0 0.0 1.0
C 6:PRO383 4.2 0.0 1.0
ND2 6:ASN365 4.3 0.0 1.0
CB 6:CYS360 4.4 0.0 1.0
C 6:CYS385 4.4 0.0 1.0
N 6:PRO383 4.5 0.0 1.0
N 6:ILE386 4.8 0.0 1.0
N 6:CYS363 4.8 0.0 1.0
CA 6:CYS363 4.8 0.0 1.0
CA 6:PRO383 4.9 0.0 1.0
O 6:PRO383 4.9 0.0 1.0
N 6:CYS382 5.0 0.0 1.0

Zinc binding site 6 out of 6 in 6o9m

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Zinc binding site 6 out of 6 in the Structure of the Human Apo Tfiih


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Structure of the Human Apo Tfiih within 5.0Å range:
probe atom residue distance (Å) B Occ
6:Zn403

b:0.0
occ:1.00
 N 6:CYS294 2.2 0.0 1.0
C 6:GLN293 2.4 0.0 1.0
CB 6:CYS308 2.5 0.0 1.0
CA 6:CYS308 2.8 0.0 1.0
O 6:GLN293 2.8 0.0 1.0
CA 6:CYS294 2.9 0.0 1.0
CB 6:GLN293 3.0 0.0 1.0
NE 1:ARG473 3.1 0.0 1.0
CZ 1:ARG473 3.1 0.0 1.0
CA 6:GLN293 3.3 0.0 1.0
CB 6:CYS294 3.4 0.0 1.0
CD 1:ARG473 3.4 0.0 1.0
NH1 1:ARG473 3.4 0.0 1.0
N 6:CYS308 3.4 0.0 1.0
NH2 1:ARG473 3.7 0.0 1.0
C 6:CYS308 4.1 0.0 1.0
C 6:ILE307 4.2 0.0 1.0
SG 6:CYS308 4.2 0.0 1.0
O 6:ILE307 4.3 0.0 1.0
C 6:CYS294 4.3 0.0 1.0
N 6:GLN293 4.3 0.0 1.0
O 6:CYS308 4.4 0.0 1.0
CG 6:GLN293 4.5 0.0 1.0
N 6:ARG295 4.9 0.0 1.0
CG 1:ARG473 4.9 0.0 1.0
SG 6:CYS294 4.9 0.0 1.0

Reference:

C.Yan, T.Dodd, Y.He, J.A.Tainer, S.E.Tsutakawa, I.Ivanov. Transcription Preinitiation Complex Structure and Dynamics Provide Insight Into Genetic Diseases. Nat.Struct.Mol.Biol. V. 26 397 2019.
ISSN: ESSN 1545-9985
PubMed: 31110295
DOI: 10.1038/S41594-019-0220-3
Page generated: Wed Dec 16 12:25:32 2020

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