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Copper in PDB 1f1a: Crystal Structure of Yeast H48Q Cuznsod Fals Mutant Analog

Enzymatic activity of Crystal Structure of Yeast H48Q Cuznsod Fals Mutant Analog

All present enzymatic activity of Crystal Structure of Yeast H48Q Cuznsod Fals Mutant Analog:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Yeast H48Q Cuznsod Fals Mutant Analog, PDB code: 1f1a was solved by P.J.Hart, N.L.Ogihara, H.Liu, A.M.Nersissian, J.S.Valentine, D.Eisenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 118.800, 118.800, 75.000, 90.00, 90.00, 120.00
R / Rfree (%) 20 / 23.3

Other elements in 1f1a:

The structure of Crystal Structure of Yeast H48Q Cuznsod Fals Mutant Analog also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Yeast H48Q Cuznsod Fals Mutant Analog (pdb code 1f1a). 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 Crystal Structure of Yeast H48Q Cuznsod Fals Mutant Analog, PDB code: 1f1a:

Copper binding site 1 out of 1 in 1f1a

Go back to Copper Binding Sites List in 1f1a
Copper binding site 1 out of 1 in the Crystal Structure of Yeast H48Q Cuznsod Fals Mutant Analog


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Yeast H48Q Cuznsod Fals Mutant Analog within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu154

b:13.8
occ:1.00
O A:HOH234 1.9 9.6 1.0
NE2 A:HIS63 2.1 12.1 1.0
NE2 A:HIS120 2.1 11.2 1.0
ND1 A:HIS46 2.1 11.6 1.0
O A:HOH197 2.3 17.1 1.0
CD2 A:HIS120 3.0 11.7 1.0
CD2 A:HIS63 3.1 11.2 1.0
CE1 A:HIS46 3.1 11.0 1.0
CE1 A:HIS120 3.1 11.4 1.0
CE1 A:HIS63 3.1 11.8 1.0
CG A:HIS46 3.1 11.1 1.0
CB A:HIS46 3.5 9.9 1.0
OE1 A:GLN48 3.5 18.2 1.0
O A:HOH217 4.2 17.9 1.0
NE2 A:HIS46 4.2 10.6 1.0
CG A:HIS120 4.2 11.1 1.0
ND1 A:HIS120 4.2 11.8 1.0
CG A:HIS63 4.2 11.0 1.0
ND1 A:HIS63 4.2 12.1 1.0
CD2 A:HIS46 4.2 12.0 1.0
O A:HOH195 4.5 15.8 1.0
CD A:GLN48 4.6 16.7 1.0
O A:THR137 4.6 14.7 1.0
CA A:HIS46 4.9 9.2 1.0
NE2 A:GLN48 4.9 16.3 1.0
CB A:ALA140 5.0 11.5 1.0

Reference:

P.J.Hart, M.M.Balbirnie, N.L.Ogihara, A.M.Nersissian, M.S.Weiss, J.S.Valentine, D.Eisenberg. A Structure-Based Mechanism For Copper-Zinc Superoxide Dismutase. Biochemistry V. 38 2167 1999.
ISSN: ISSN 0006-2960
PubMed: 10026301
DOI: 10.1021/BI982284U
Page generated: Wed Oct 28 14:14:21 2020
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