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Zinc in PDB 5gpy: Crystal Structure of the Human Tfiie Complex

Protein crystallography data

The structure of Crystal Structure of the Human Tfiie Complex, PDB code: 5gpy was solved by T.Obita, K.Miwa, R.Kojima, Y.Ohkuma, Y.Tamura, M.Mizuguchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.33 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.520, 69.200, 116.530, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 23.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Human Tfiie Complex (pdb code 5gpy). 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 Human Tfiie Complex, PDB code: 5gpy:

Zinc binding site 1 out of 1 in 5gpy

Go back to Zinc Binding Sites List in 5gpy
Zinc binding site 1 out of 1 in the Crystal Structure of the Human Tfiie Complex


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 Human Tfiie Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:57.0
occ:1.00
SG A:CYS132 2.3 42.5 1.0
SG A:CYS157 2.4 53.6 1.0
SG A:CYS154 2.4 52.7 1.0
SG A:CYS129 2.4 51.4 1.0
CB A:CYS129 3.1 44.3 1.0
CB A:CYS154 3.2 50.4 1.0
CB A:CYS157 3.4 51.5 1.0
CB A:CYS132 3.4 50.8 1.0
N A:CYS157 3.7 58.5 1.0
N A:CYS132 3.9 49.0 1.0
CA A:CYS157 4.1 56.1 1.0
CA A:CYS132 4.2 50.0 1.0
CA A:CYS129 4.6 49.1 1.0
CB A:PHE156 4.7 51.1 1.0
CA A:CYS154 4.7 53.2 1.0
C A:CYS157 4.7 62.0 1.0
N A:HIS158 4.8 68.5 1.0
CB A:VAL131 4.8 49.8 1.0
CB A:SER134 4.8 44.4 1.0
C A:PHE156 4.8 62.1 1.0
CB A:THR159 4.8 60.4 1.0
C A:CYS132 4.8 45.2 1.0
OG A:SER134 4.9 45.9 1.0
N A:SER133 4.9 43.7 1.0
N A:THR159 5.0 62.5 1.0

Reference:

K.Miwa, R.Kojima, T.Obita, Y.Ohkuma, Y.Tamura, M.Mizuguchi. Crystal Structure of Human General Transcription Factor Tfiie at Atomic Resolution J.Mol.Biol. V. 428 4258 2016.
ISSN: ESSN 1089-8638
PubMed: 27639436
DOI: 10.1016/J.JMB.2016.09.008
Page generated: Wed Dec 16 06:19:43 2020

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