Copper in PDB 2zhp: Crystal Structure of Bleomycin-Binding Protein From Streptoalloteichus Hindustanus Complexed with Bleomycin Derivative

The structure of Crystal Structure of Bleomycin-Binding Protein From Streptoalloteichus Hindustanus Complexed with Bleomycin Derivative, PDB code: 2zhp was solved by H.Okumura, I.Miyazaki, S.Simizu, H.Osada, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.11 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.992, 53.868, 125.498, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 21.6

The structure of Crystal Structure of Bleomycin-Binding Protein From Streptoalloteichus Hindustanus Complexed with Bleomycin Derivative also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Copper atom in the Crystal Structure of Bleomycin-Binding Protein From Streptoalloteichus Hindustanus Complexed with Bleomycin Derivative (pdb code 2zhp). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Bleomycin-Binding Protein From Streptoalloteichus Hindustanus Complexed with Bleomycin Derivative, PDB code: 2zhp:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Bleomycin-Binding Protein From Streptoalloteichus Hindustanus Complexed with Bleomycin Derivative


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 Bleomycin-Binding Protein From Streptoalloteichus Hindustanus Complexed with Bleomycin Derivative within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu302 b:12.9 occ:1.00 NG A:BY6301 2.0 6.6 1.0 NJ A:BY6301 2.0 5.5 1.0 NH A:BY6301 2.2 10.3 1.0 NC A:BY6301 2.2 10.8 1.0 NB A:BY6301 2.4 12.8 1.0 C7 A:BY6301 2.8 9.4 1.0 C10 A:BY6301 2.8 6.6 1.0 C29 A:BY6301 2.9 11.2 1.0 C12 A:BY6301 2.9 8.4 1.0 C6 A:BY6301 3.0 10.8 1.0 C3 A:BY6301 3.0 6.6 1.0 C27 A:BY6301 3.0 8.4 1.0 C2 A:BY6301 3.1 12.2 1.0 C13 A:BY6301 3.4 9.8 1.0 C1 A:BY6301 3.4 15.6 1.0 C14 A:BY6301 3.5 9.3 1.0 OH1 A:BY6301 3.5 10.2 1.0 CL A:CL303 3.7 19.6 1.0 OH3 A:BY6301 3.8 13.2 1.0 O1 A:BY6301 3.9 18.5 1.0 NA A:BY6301 3.9 18.1 1.0 NI A:BY6301 4.0 9.0 1.0 NE A:BY6301 4.0 7.9 1.0 C28 A:BY6301 4.1 9.6 1.0 O70 A:BY6301 4.1 10.8 1.0 O12 A:BY6301 4.2 9.7 1.0 NK A:BY6301 4.2 8.8 1.0 C30 A:BY6301 4.2 9.6 1.0 C9 A:BY6301 4.2 7.4 1.0 O A:HOH578 4.4 26.1 1.0 C5 A:BY6301 4.5 8.9 1.0 C8 A:BY6301 4.7 9.0 1.0 C63 A:BY6301 4.8 12.4 1.0 NL A:BY6301 4.8 7.2 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Bleomycin-Binding Protein From Streptoalloteichus Hindustanus Complexed with Bleomycin Derivative


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Bleomycin-Binding Protein From Streptoalloteichus Hindustanus Complexed with Bleomycin Derivative within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu402 b:17.1 occ:1.00 NG B:BY6401 1.9 8.4 1.0 NJ B:BY6401 2.1 24.6 1.0 NH B:BY6401 2.2 18.6 1.0 NC B:BY6401 2.3 14.0 1.0 NB B:BY6401 2.3 22.1 1.0 C7 B:BY6401 2.8 13.4 1.0 C10 B:BY6401 2.8 13.3 1.0 C12 B:BY6401 2.9 16.6 1.0 C6 B:BY6401 3.0 12.2 1.0 C3 B:BY6401 3.0 17.4 1.0 C2 B:BY6401 3.1 27.7 1.0 C27 B:BY6401 3.1 25.6 1.0 C29 B:BY6401 3.1 21.5 1.0 C13 B:BY6401 3.4 20.8 1.0 C1 B:BY6401 3.5 27.1 1.0 C14 B:BY6401 3.5 24.6 1.0 CL B:CL403 3.5 25.8 1.0 OH1 B:BY6401 3.5 27.4 1.0 NA B:BY6401 3.9 29.1 1.0 O1 B:BY6401 3.9 25.2 1.0 OH3 B:BY6401 4.0 20.6 1.0 NE B:BY6401 4.0 8.8 1.0 O12 B:BY6401 4.1 18.2 1.0 NK B:BY6401 4.1 16.1 1.0 C9 B:BY6401 4.2 11.1 1.0 NI B:BY6401 4.2 25.8 1.0 C30 B:BY6401 4.2 21.1 1.0 O70 B:BY6401 4.2 31.6 1.0 C28 B:BY6401 4.2 30.7 1.0 C5 B:BY6401 4.5 14.2 1.0 C8 B:BY6401 4.6 9.4 1.0 NL B:BY6401 4.8 15.2 1.0 C63 B:BY6401 4.9 36.1 1.0 O58 B:BY6401 5.0 41.4 1.0

I.Miyazaki, H.Okumura, S.Simizu, Y.Takahashi, N.Kanoh, Y.Nonomura, H.Osada. Structure-Affinity Relationship Study of Bleomycins and Shble Protein Using A Chemical Array To Be Published.