Copper in PDB 9h9z: Crystal Structure of Cu(II)-Bound LMRR_V15BPY

The structure of Crystal Structure of Cu(II)-Bound LMRR_V15BPY, PDB code: 9h9z was solved by A.M.W.H.Thunnissen, R.Jiang, F.Casilli, F.Aalbers, G.Roelfes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.51 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	35.496, 53.359, 147.778, 90, 90, 90
R / Rfree (%)	20.2 / 23.9

The binding sites of Copper atom in the Crystal Structure of Cu(II)-Bound LMRR_V15BPY (pdb code 9h9z). 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 Cu(II)-Bound LMRR_V15BPY, PDB code: 9h9z:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Cu(II)-Bound LMRR_V15BPY


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 Cu(II)-Bound LMRR_V15BPY within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:81.6 occ:1.00 O A:HOH329 1.9 60.8 1.0 N2 A:BP515 2.0 53.8 1.0 N1 A:BP515 2.0 74.8 1.0 O A:HOH332 2.0 72.5 1.0 C3 A:BP515 2.8 64.9 1.0 C6 A:BP515 2.8 43.0 1.0 C11 A:BP515 3.0 43.2 1.0 C4 A:BP515 3.0 77.7 1.0 H11 A:BP515 3.1 51.9 1.0 H4 A:BP515 3.2 93.2 1.0 HD21 A:ASN19 3.2 54.7 1.0 ND2 A:ASN19 4.0 45.6 1.0 O B:HOH329 4.1 49.0 1.0 C2 A:BP515 4.1 64.3 1.0 C7 A:BP515 4.1 45.7 1.0 C9 A:BP515 4.3 34.0 1.0 C5 A:BP515 4.3 71.9 1.0 HD22 A:ASN19 4.4 54.7 1.0 C8 A:BP515 4.7 36.1 1.0 C1 A:BP515 4.7 60.7 1.0 H3 A:BP515 4.8 77.1 1.0 HE3 A:MET89 4.9 82.8 1.0 CG A:ASN19 4.9 55.9 1.0 OD1 A:ASN19 4.9 50.2 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Cu(II)-Bound LMRR_V15BPY


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 Cu(II)-Bound LMRR_V15BPY within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu202 b:56.5 occ:1.00 N2 B:BP515 2.0 46.4 1.0 N1 B:BP515 2.0 55.7 1.0 O B:HOH301 2.0 67.2 1.0 O9 B:MLI201 2.1 68.7 1.0 O B:HOH313 2.1 43.5 1.0 O7 B:MLI201 2.1 69.5 1.0 C6 B:BP515 2.8 43.4 1.0 C3 B:BP515 2.8 49.1 1.0 C3 B:MLI201 2.9 56.1 1.0 C2 B:MLI201 3.0 55.4 1.0 C11 B:BP515 3.0 35.3 1.0 H11 B:MLI201 3.1 53.9 1.0 C4 B:BP515 3.1 54.3 1.0 C1 B:MLI201 3.1 44.9 1.0 H11 B:BP515 3.1 42.4 1.0 H4 B:BP515 3.2 65.2 1.0 HD21 B:ASN19 3.9 40.4 1.0 O8 B:MLI201 4.0 59.5 1.0 H12 B:MLI201 4.1 53.9 1.0 C7 B:BP515 4.1 40.8 1.0 C2 B:BP515 4.1 48.8 1.0 O6 B:MLI201 4.2 53.6 1.0 C9 B:BP515 4.3 32.9 1.0 C5 B:BP515 4.3 48.8 1.0 ND2 B:ASN19 4.7 33.7 1.0 OD1 A:ASP100 4.7 46.0 1.0 C8 B:BP515 4.7 36.4 1.0 C1 B:BP515 4.8 44.7 1.0 H3 B:BP515 4.8 58.6 1.0

R.Jiang, F.Casilli, A.W.H.Thunnissen, G.Roelfes. An Artificial Copper-Michaelase Featuring A Genetically Encoded Bipyridine Ligand For Asymmetric Additions to Nitroalkenes. Angew.Chem.Int.Ed.Engl. 23182 2025.
ISSN: ESSN 1521-3773
PubMed: 39945539
DOI: 10.1002/ANIE.202423182