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Zinc in PDB 3poa: Structural and Functional Analysis of Phosphothreonine-Dependent Fha Domain Interactions

Protein crystallography data

The structure of Structural and Functional Analysis of Phosphothreonine-Dependent Fha Domain Interactions, PDB code: 3poa was solved by S.Pennell, S.J.Smerdon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.05 / 2.01
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 57.016, 74.425, 63.016, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 23.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural and Functional Analysis of Phosphothreonine-Dependent Fha Domain Interactions (pdb code 3poa). 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 Structural and Functional Analysis of Phosphothreonine-Dependent Fha Domain Interactions, PDB code: 3poa:

Zinc binding site 1 out of 1 in 3poa

Go back to Zinc Binding Sites List in 3poa
Zinc binding site 1 out of 1 in the Structural and Functional Analysis of Phosphothreonine-Dependent Fha Domain Interactions


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural and Functional Analysis of Phosphothreonine-Dependent Fha Domain Interactions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn101

b:15.3
occ:1.00
O A:HOH208 1.9 14.0 1.0
OD2 A:ASP81 2.1 14.8 1.0
NE2 A:HIS97 2.2 16.5 1.0
OD1 A:ASP81 2.7 14.6 1.0
CG A:ASP81 2.7 15.4 1.0
CD2 A:HIS97 2.8 15.7 1.0
CE1 A:HIS97 3.3 16.5 1.0
CG A:HIS97 4.1 17.9 1.0
CB A:ASP81 4.2 15.2 1.0
O A:HOH291 4.2 33.3 1.0
ND1 A:HIS97 4.3 18.4 1.0
O A:MET96 4.7 18.1 1.0
N A:MET96 4.9 16.6 1.0

Reference:

S.Pennell, S.Westcott, M.Ortiz-Lombardia, D.Patel, J.Li, T.J.Nott, D.Mohammed, R.S.Buxton, M.B.Yaffe, C.Verma, S.J.Smerdon. Structural and Functional Analysis of Phosphothreonine-Dependent Fha Domain Interactions Structure V. 18 1587 2010.
ISSN: ISSN 0969-2126
PubMed: 21134638
DOI: 10.1016/J.STR.2010.09.014
Page generated: Wed Dec 16 04:43:39 2020

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