Atomistry » Copper » PDB 1eso-1haw » 1f1a
Atomistry »
  Copper »
    PDB 1eso-1haw »
      1f1a »

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: Tue Jul 30 21:46:54 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy