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Zinc in PDB 2l1u: Structure-Functional Analysis of Mammalian MSRB2 Protein

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure-Functional Analysis of Mammalian MSRB2 Protein (pdb code 2l1u). 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 Structure-Functional Analysis of Mammalian MSRB2 Protein, PDB code: 2l1u:

Zinc binding site 1 out of 1 in 2l1u

Go back to Zinc Binding Sites List in 2l1u
Zinc binding site 1 out of 1 in the Structure-Functional Analysis of Mammalian MSRB2 Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure-Functional Analysis of Mammalian MSRB2 Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn144

b:0.0
occ:1.00
SG A:CYS43 2.3 0.0 1.0
SG A:CYS96 2.4 0.0 1.0
SG A:CYS99 2.4 0.0 1.0
SG A:CYS40 2.4 0.0 1.0
HB2 A:GLN98 3.0 0.0 1.0
OG A:SER45 3.3 0.0 1.0
H A:CYS99 3.5 0.0 1.0
HG A:SER45 3.6 0.0 1.0
HB3 A:CYS99 3.6 0.0 1.0
HB2 A:CYS40 3.6 0.0 1.0
CB A:CYS96 3.6 0.0 1.0
CB A:CYS40 3.7 0.0 1.0
HB2 A:CYS96 3.7 0.0 1.0
CB A:CYS99 3.7 0.0 1.0
CB A:CYS43 3.8 0.0 1.0
H A:SER45 3.8 0.0 1.0
HB3 A:CYS96 3.9 0.0 1.0
HB3 A:CYS43 3.9 0.0 1.0
HB3 A:CYS40 4.0 0.0 1.0
H A:ASP44 4.0 0.0 1.0
CB A:GLN98 4.1 0.0 1.0
HB2 A:CYS43 4.1 0.0 1.0
N A:CYS99 4.2 0.0 1.0
HD22 A:LEU47 4.2 0.0 1.0
HG3 A:GLN98 4.3 0.0 1.0
H A:CYS43 4.3 0.0 1.0
H A:CYS40 4.4 0.0 1.0
HB2 A:CYS99 4.5 0.0 1.0
O A:SER45 4.5 0.0 1.0
H A:GLN98 4.6 0.0 1.0
HB3 A:GLN98 4.6 0.0 1.0
CB A:SER45 4.6 0.0 1.0
N A:SER45 4.6 0.0 1.0
CA A:CYS99 4.7 0.0 1.0
CG A:GLN98 4.7 0.0 1.0
HB2 A:ALA101 4.7 0.0 1.0
OE1 A:GLN98 4.7 0.0 1.0
C A:GLN98 4.9 0.0 1.0
CA A:GLN98 4.9 0.0 1.0
HG A:LEU47 4.9 0.0 1.0
CA A:CYS96 5.0 0.0 1.0
HD23 A:LEU47 5.0 0.0 1.0
CA A:CYS43 5.0 0.0 1.0
HB2 A:SER45 5.0 0.0 1.0
N A:CYS43 5.0 0.0 1.0
CA A:CYS40 5.0 0.0 1.0

Reference:

F.L.Aachmann, R.Del Conte, G.Kwak, H.Kim, V.N.Gladyshev, A.Dikiy. Structure-Functional Analysis of Mammalian MSRB2 Protein To Be Published.
Page generated: Thu Oct 17 01:44:08 2024

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