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Zinc in PDB 2rmn: The Solution Structure of the P63 Dna-Binding Domain

Zinc Binding Sites:

The binding sites of Zinc atom in the The Solution Structure of the P63 Dna-Binding Domain (pdb code 2rmn). 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 The Solution Structure of the P63 Dna-Binding Domain, PDB code: 2rmn:

Zinc binding site 1 out of 1 in 2rmn

Go back to Zinc Binding Sites List in 2rmn
Zinc binding site 1 out of 1 in the The Solution Structure of the P63 Dna-Binding Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Solution Structure of the P63 Dna-Binding Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:0.0
occ:1.00
SG A:CYS205 2.1 0.0 1.0
SG A:CYS269 2.2 0.0 1.0
ND1 A:HIS208 2.2 0.0 1.0
SG A:CYS273 2.2 0.0 1.0
HB2 A:CYS205 3.1 0.0 1.0
HB2 A:CYS273 3.1 0.0 1.0
CE1 A:HIS208 3.1 0.0 1.0
HE1 A:HIS208 3.2 0.0 1.0
CB A:CYS205 3.2 0.0 1.0
HB2 A:HIS208 3.3 0.0 1.0
CB A:CYS273 3.3 0.0 1.0
CG A:HIS208 3.3 0.0 1.0
HB3 A:CYS269 3.3 0.0 1.0
CB A:CYS269 3.4 0.0 1.0
H A:CYS205 3.5 0.0 1.0
H A:ASN270 3.6 0.0 1.0
HA A:CYS269 3.7 0.0 1.0
CB A:HIS208 3.7 0.0 1.0
HB3 A:CYS273 3.8 0.0 1.0
HB3 A:CYS205 3.9 0.0 1.0
HB3 A:HIS208 3.9 0.0 1.0
CA A:CYS269 4.1 0.0 1.0
HA3 A:GLY276 4.1 0.0 1.0
N A:CYS205 4.2 0.0 1.0
HB2 A:CYS269 4.2 0.0 1.0
O A:CYS273 4.3 0.0 1.0
NE2 A:HIS208 4.3 0.0 1.0
CD2 A:HIS208 4.4 0.0 1.0
N A:ASN270 4.4 0.0 1.0
CA A:CYS205 4.4 0.0 1.0
CA A:CYS273 4.5 0.0 1.0
HD22 A:ASN207 4.6 0.0 1.0
C A:CYS273 4.7 0.0 1.0
OD1 A:ASN207 4.7 0.0 1.0
O A:ASN270 4.7 0.0 1.0
C A:CYS269 4.7 0.0 1.0
H A:MET277 4.8 0.0 1.0
H A:HIS208 4.8 0.0 1.0
H A:CYS273 4.9 0.0 1.0
OD1 A:ASN270 4.9 0.0 1.0
H A:GLY276 4.9 0.0 1.0
HA A:CYS205 5.0 0.0 1.0

Reference:

A.Enthart, C.Klein, A.Dehner, M.Coles, G.Gemmecker, H.Kessler, F.Hagn. Solution Structure and Binding Specificity of the P63 Dna Binding Domain Sci Rep V. 6 26707 2016.
ISSN: ESSN 2045-2322
PubMed: 27225672
DOI: 10.1038/SREP26707
Page generated: Sat Sep 26 03:52:29 2020
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