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Zinc in PDB 4bcy: Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F

Enzymatic activity of Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F

All present enzymatic activity of Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F:
1.15.1.1;

Protein crystallography data

The structure of Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F, PDB code: 4bcy was solved by W.Awad, K.Saraboji, J.Danielsson, L.Lang, M.Kurnik, S.L.Marklund, M.Oliveberg, D.T.Logan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.19 / 1.27
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 34.870, 47.910, 81.180, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 20.3

Other elements in 4bcy:

The structure of Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F also contains other interesting chemical elements:

Cadmium (Cd) 6 atoms
Copper (Cu) 2 atoms
Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F (pdb code 4bcy). 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 Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F, PDB code: 4bcy:

Zinc binding site 1 out of 1 in 4bcy

Go back to Zinc Binding Sites List in 4bcy
Zinc binding site 1 out of 1 in the Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1155

b:18.3
occ:0.87
OD1 A:ASP83 2.0 18.4 1.0
ND1 A:HIS63 2.0 19.1 1.0
ND1 A:HIS71 2.1 18.6 1.0
ND1 A:HIS80 2.1 20.4 1.0
CG A:ASP83 2.7 18.5 1.0
OD2 A:ASP83 2.8 19.5 1.0
CE1 A:HIS80 2.9 19.9 1.0
CE1 A:HIS71 2.9 20.6 1.0
CE1 A:HIS63 3.0 21.5 1.0
CG A:HIS63 3.1 21.0 1.0
CG A:HIS80 3.1 19.0 1.0
CG A:HIS71 3.2 18.3 1.0
CB A:HIS63 3.4 19.8 1.0
CB A:HIS80 3.6 18.5 1.0
CB A:HIS71 3.6 19.8 1.0
O A:LYS136 3.8 20.8 1.0
CA A:HIS71 3.9 19.7 1.0
NE2 A:HIS80 4.1 19.8 1.0
NE2 A:HIS63 4.1 23.1 1.0
NE2 A:HIS71 4.1 19.9 1.0
CB A:ASP83 4.2 19.3 1.0
CD2 A:HIS63 4.2 23.2 1.0
CD2 A:HIS80 4.2 19.4 1.0
CD2 A:HIS71 4.3 20.8 1.0
CA A:ASP83 4.7 19.3 1.0
N A:HIS80 4.7 19.2 1.0
N A:GLY72 4.7 21.6 1.0
CA A:HIS80 4.8 19.1 1.0
C A:LYS136 4.8 20.2 1.0
C A:HIS71 4.9 20.7 1.0
N A:HIS71 4.9 21.6 1.0
N A:ASP83 4.9 17.8 1.0
CA A:HIS63 5.0 19.1 1.0
O A:HOH2024 5.0 24.8 1.0

Reference:

J.Danielsson, W.Awad, K.Saraboji, M.Kurnik, L.Lang, L.Leinartaite, S.L.Marklund, D.T.Logan, M.Oliveberg. Global Structural Motions From the Strain of A Single Hydrogen Bond. Proc.Natl.Acad.Sci.Usa V. 110 3829 2013.
ISSN: ISSN 0027-8424
PubMed: 23431167
DOI: 10.1073/PNAS.1217306110
Page generated: Wed Dec 16 05:05:03 2020

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