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Zinc in PDB 1i27: Crystal Structure of the C-Terminal Domain of the RAP74 Subunit of Human Transcription Factor Iif (Tfiif)

Protein crystallography data

The structure of Crystal Structure of the C-Terminal Domain of the RAP74 Subunit of Human Transcription Factor Iif (Tfiif), PDB code: 1i27 was solved by K.Kamada, J.De Angelis, R.G.Roeder, S.K.Burley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.02
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 29.052, 43.024, 48.161, 90.00, 90.00, 90.00
R / Rfree (%) 12.6 / 14.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the C-Terminal Domain of the RAP74 Subunit of Human Transcription Factor Iif (Tfiif) (pdb code 1i27). 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 Crystal Structure of the C-Terminal Domain of the RAP74 Subunit of Human Transcription Factor Iif (Tfiif), PDB code: 1i27:

Zinc binding site 1 out of 1 in 1i27

Go back to Zinc Binding Sites List in 1i27
Zinc binding site 1 out of 1 in the Crystal Structure of the C-Terminal Domain of the RAP74 Subunit of Human Transcription Factor Iif (Tfiif)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the C-Terminal Domain of the RAP74 Subunit of Human Transcription Factor Iif (Tfiif) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn999

b:8.8
occ:1.00
NE2 A:HIS512 2.0 7.1 1.0
O A:HOH1001 2.0 12.9 1.0
CE1 A:HIS512 3.0 7.1 1.0
CD2 A:HIS512 3.0 6.9 1.0
ND1 A:HIS512 4.1 6.9 1.0
OD1 A:ASP472 4.1 9.2 1.0
CG A:HIS512 4.2 6.8 1.0
ND2 A:ASN508 4.4 8.7 1.0
O A:HOH1058 4.4 14.3 1.0
CG2 A:THR469 4.5 9.1 1.0
CG2 A:ILE507 4.5 11.9 1.0
O A:HOH1057 4.7 27.6 1.0
CB A:ILE507 5.0 8.6 1.0

Reference:

K.Kamada, J.De Angelis, R.G.Roeder, S.K.Burley. Crystal Structure of the C-Terminal Domain of the RAP74 Subunit of Human Transcription Factor Iif. Proc.Natl.Acad.Sci.Usa V. 98 3115 2001.
ISSN: ISSN 0027-8424
PubMed: 11248041
DOI: 10.1073/PNAS.051631098
Page generated: Wed Dec 16 02:52:13 2020

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