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Zinc in PDB 1ba9: The Solution Structure of Reduced Monomeric Superoxide Dismutase, uc(Nmr), 36 Structures

Enzymatic activity of The Solution Structure of Reduced Monomeric Superoxide Dismutase, uc(Nmr), 36 Structures

All present enzymatic activity of The Solution Structure of Reduced Monomeric Superoxide Dismutase, uc(Nmr), 36 Structures:
1.15.1.1;

Other elements in 1ba9:

The structure of The Solution Structure of Reduced Monomeric Superoxide Dismutase, uc(Nmr), 36 Structures also contains other interesting chemical elements:

Copper (Cu) 36 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the The Solution Structure of Reduced Monomeric Superoxide Dismutase, uc(Nmr), 36 Structures (pdb code 1ba9). 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 Reduced Monomeric Superoxide Dismutase, uc(Nmr), 36 Structures, PDB code: 1ba9:

Zinc binding site 1 out of 1 in 1ba9

Go back to Zinc Binding Sites List in 1ba9
Zinc binding site 1 out of 1 in the The Solution Structure of Reduced Monomeric Superoxide Dismutase, uc(Nmr), 36 Structures


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 Reduced Monomeric Superoxide Dismutase, uc(Nmr), 36 Structures within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn154

b:0.0
occ:1.00
OD1 A:ASP83 1.9 0.0 1.0
ND1 A:HIS71 2.0 0.0 1.0
ND1 A:HIS80 2.0 0.0 1.0
ND1 A:HIS63 2.1 0.0 1.0
OD2 A:ASP83 2.4 0.0 1.0
CG A:ASP83 2.4 0.0 1.0
CE1 A:HIS71 2.9 0.0 1.0
CE1 A:HIS80 3.0 0.0 1.0
HE1 A:HIS71 3.0 0.0 1.0
CG A:HIS80 3.1 0.0 1.0
HB3 A:HIS63 3.1 0.0 1.0
CE1 A:HIS63 3.1 0.0 1.0
CG A:HIS71 3.1 0.0 1.0
HB2 A:HIS80 3.1 0.0 1.0
HA A:HIS71 3.2 0.0 1.0
CG A:HIS63 3.2 0.0 1.0
HE1 A:HIS80 3.2 0.0 1.0
HE1 A:HIS63 3.3 0.0 1.0
H A:GLY72 3.6 0.0 1.0
CB A:HIS80 3.6 0.0 1.0
CB A:HIS63 3.6 0.0 1.0
HB2 A:HIS71 3.7 0.0 1.0
H A:HIS80 3.7 0.0 1.0
CB A:HIS71 3.7 0.0 1.0
CB A:ASP83 3.9 0.0 1.0
O A:LYS136 3.9 0.0 1.0
CA A:HIS71 3.9 0.0 1.0
NE2 A:HIS71 4.0 0.0 1.0
NE2 A:HIS80 4.0 0.0 1.0
HA A:ASP83 4.1 0.0 1.0
HB2 A:HIS63 4.1 0.0 1.0
CD2 A:HIS80 4.1 0.0 1.0
CD2 A:HIS71 4.1 0.0 1.0
NE2 A:HIS63 4.2 0.0 1.0
HB3 A:ASP83 4.3 0.0 1.0
CD2 A:HIS63 4.3 0.0 1.0
HB3 A:HIS80 4.4 0.0 1.0
N A:GLY72 4.5 0.0 1.0
N A:HIS80 4.5 0.0 1.0
HA A:THR137 4.5 0.0 1.0
CA A:ASP83 4.5 0.0 1.0
HB2 A:ASP83 4.5 0.0 1.0
HD2 A:HIS46 4.6 0.0 1.0
HB3 A:HIS46 4.6 0.0 1.0
CA A:HIS80 4.7 0.0 1.0
C A:LYS136 4.8 0.0 1.0
O A:GLY72 4.8 0.0 1.0
HB3 A:HIS71 4.8 0.0 1.0
C A:HIS71 4.8 0.0 1.0
HE2 A:HIS71 4.8 0.0 1.0
CD2 A:HIS46 4.8 0.0 1.0
HE2 A:HIS80 4.9 0.0 1.0
CA A:HIS63 5.0 0.0 1.0
N A:ASP83 5.0 0.0 1.0
N A:HIS71 5.0 0.0 1.0

Reference:

L.Banci, M.Benedetto, I.Bertini, R.Del Conte, M.Piccioli, M.S.Viezzoli. Solution Structure of Reduced Monomeric Q133M2 Copper, Zinc Superoxide Dismutase (Sod). Why Is Sod A Dimeric Enzyme?. Biochemistry V. 37 11780 1998.
ISSN: ISSN 0006-2960
PubMed: 9718300
DOI: 10.1021/BI9803473
Page generated: Sat Oct 12 22:28:19 2024

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