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Copper in PDB 2lu5: Structure and Chemical Shifts of Cu(I),Zn(II) Superoxide Dismutase By Solid-State uc(Nmr)

Enzymatic activity of Structure and Chemical Shifts of Cu(I),Zn(II) Superoxide Dismutase By Solid-State uc(Nmr)

All present enzymatic activity of Structure and Chemical Shifts of Cu(I),Zn(II) Superoxide Dismutase By Solid-State uc(Nmr):
1.15.1.1;

Copper Binding Sites:

The binding sites of Copper atom in the Structure and Chemical Shifts of Cu(I),Zn(II) Superoxide Dismutase By Solid-State uc(Nmr) (pdb code 2lu5). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Structure and Chemical Shifts of Cu(I),Zn(II) Superoxide Dismutase By Solid-State uc(Nmr), PDB code: 2lu5:

Copper binding site 1 out of 1 in 2lu5

Go back to Copper Binding Sites List in 2lu5
Copper binding site 1 out of 1 in the Structure and Chemical Shifts of Cu(I),Zn(II) Superoxide Dismutase By Solid-State uc(Nmr)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure and Chemical Shifts of Cu(I),Zn(II) Superoxide Dismutase By Solid-State uc(Nmr) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:0.0
occ:1.00
OD1 A:ASP124 1.6 0.0 1.0
OD2 A:ASP124 1.6 0.0 1.0
O A:ASN139 1.9 0.0 1.0
CG A:ASP124 2.0 0.0 1.0
O A:HIS46 2.1 0.0 1.0
O A:VAL118 2.5 0.0 1.0
HA A:ALA140 2.7 0.0 1.0
HG21 A:VAL118 2.9 0.0 1.0
HB3 A:HIS46 2.9 0.0 1.0
C A:ASN139 3.2 0.0 1.0
C A:HIS46 3.2 0.0 1.0
HB A:VAL118 3.3 0.0 1.0
H A:HIS46 3.4 0.0 1.0
CB A:ASP124 3.5 0.0 1.0
C A:VAL118 3.6 0.0 1.0
HB2 A:ALA140 3.6 0.0 1.0
CA A:ALA140 3.6 0.0 1.0
CG2 A:VAL118 3.7 0.0 1.0
CB A:HIS46 3.8 0.0 1.0
N A:ALA140 3.8 0.0 1.0
CA A:HIS46 3.9 0.0 1.0
HG23 A:VAL118 3.9 0.0 1.0
CB A:VAL118 3.9 0.0 1.0
HB2 A:ASP124 4.0 0.0 1.0
HB3 A:ASP124 4.0 0.0 1.0
HA A:VAL119 4.0 0.0 1.0
HD1 A:HIS46 4.0 0.0 1.0
O A:GLY138 4.0 0.0 1.0
N A:HIS46 4.0 0.0 1.0
HA A:VAL47 4.1 0.0 1.0
CB A:ALA140 4.1 0.0 1.0
N A:VAL47 4.3 0.0 1.0
H A:GLY141 4.3 0.0 1.0
CA A:VAL118 4.4 0.0 1.0
CA A:ASP124 4.4 0.0 1.0
HA A:ASP124 4.4 0.0 1.0
HB3 A:ALA140 4.4 0.0 1.0
CA A:ASN139 4.4 0.0 1.0
HB3 A:ASN139 4.4 0.0 1.0
O A:ASP124 4.4 0.0 1.0
N A:VAL119 4.5 0.0 1.0
HB2 A:HIS46 4.5 0.0 1.0
C A:ASP124 4.6 0.0 1.0
HG22 A:VAL118 4.6 0.0 1.0
ND1 A:HIS46 4.6 0.0 1.0
CG A:HIS46 4.7 0.0 1.0
C A:GLY138 4.7 0.0 1.0
CA A:VAL47 4.7 0.0 1.0
N A:ASN139 4.8 0.0 1.0
CA A:VAL119 4.8 0.0 1.0
H A:ALA140 4.8 0.0 1.0
C A:ALA140 4.9 0.0 1.0
HA A:HIS46 4.9 0.0 1.0
CB A:ASN139 4.9 0.0 1.0
N A:GLY141 5.0 0.0 1.0
H A:VAL118 5.0 0.0 1.0

Reference:

M.J.Knight, A.J.Pell, I.Bertini, I.C.Felli, L.Gonnelli, R.Pierattelli, T.Herrmann, L.Emsley, G.Pintacuda. Structure and Backbone Dynamics of A Microcrystalline Metalloprotein By Solid-State uc(Nmr). Proc.Natl.Acad.Sci.Usa V. 109 11095 2012.
ISSN: ISSN 0027-8424
PubMed: 22723345
DOI: 10.1073/PNAS.1204515109
Page generated: Wed Oct 28 14:20:41 2020
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