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Chlorine in PDB 5b1k: Crystal Structure of the Chloride-Bound Form of Blue Copper Nitrite Reductase

Enzymatic activity of Crystal Structure of the Chloride-Bound Form of Blue Copper Nitrite Reductase

All present enzymatic activity of Crystal Structure of the Chloride-Bound Form of Blue Copper Nitrite Reductase:
1.7.2.1;

Protein crystallography data

The structure of Crystal Structure of the Chloride-Bound Form of Blue Copper Nitrite Reductase, PDB code: 5b1k was solved by M.Nojiri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 90.50 / 1.35
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 104.703, 104.703, 63.073, 90.00, 90.00, 120.00
R / Rfree (%) 14.9 / 17.3

Other elements in 5b1k:

The structure of Crystal Structure of the Chloride-Bound Form of Blue Copper Nitrite Reductase also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Chloride-Bound Form of Blue Copper Nitrite Reductase (pdb code 5b1k). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Chloride-Bound Form of Blue Copper Nitrite Reductase, PDB code: 5b1k:

Chlorine binding site 1 out of 1 in 5b1k

Go back to Chlorine Binding Sites List in 5b1k
Chlorine binding site 1 out of 1 in the Crystal Structure of the Chloride-Bound Form of Blue Copper Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Chloride-Bound Form of Blue Copper Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:32.1
occ:0.75
O A:HOH501 2.5 30.0 0.8
CU A:CU402 2.5 12.1 1.0
NE2 A:HIS129 3.5 10.6 1.0
CE1 A:HIS129 3.7 11.4 1.0
OD2 A:ASP92 4.0 19.3 1.0
NE2 A:HIS94 4.4 9.6 1.0
CD2 A:HIS129 4.8 10.8 1.0
ND1 A:HIS129 5.0 11.4 1.0

Reference:

M.Nojiri, M.Nojiri. N/A N/A.
DOI: 10.1039/9781782623762-00091
Page generated: Sat Dec 12 11:31:45 2020

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