Copper in PDB 2eb9: Crystal Structure of Cu(II)(Sal-Leu)/Apo-Myoglobin

The structure of Crystal Structure of Cu(II)(Sal-Leu)/Apo-Myoglobin, PDB code: 2eb9 was solved by S.Abe, S.Okazaki, T.Ueno, T.Hikage, A.Suzuki, T.Yamane, Y.Watanabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.03 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	32.580, 57.901, 75.282, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 23.9

The binding sites of Copper atom in the Crystal Structure of Cu(II)(Sal-Leu)/Apo-Myoglobin (pdb code 2eb9). 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 Cu(II)(Sal-Leu)/Apo-Myoglobin, PDB code: 2eb9:

Copper binding site 1 out of 1 in the Crystal Structure of Cu(II)(Sal-Leu)/Apo-Myoglobin


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)(Sal-Leu)/Apo-Myoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1001 b:29.7 occ:1.00 CU1 A:CUS1001 0.0 29.7 1.0 O1 A:CUS1001 2.0 34.7 1.0 N1 A:CUS1001 2.0 34.5 1.0 NE2 A:HIS64 2.1 18.8 1.0 O2 A:CUS1001 2.1 36.1 1.0 C1 A:CUS1001 2.9 33.0 1.0 C8 A:CUS1001 3.0 37.6 1.0 C7 A:CUS1001 3.0 34.2 1.0 C9 A:CUS1001 3.0 36.3 1.0 CE1 A:HIS64 3.0 20.6 1.0 CD2 A:HIS64 3.0 18.5 1.0 C2 A:CUS1001 3.3 33.8 1.0 CG2 A:VAL68 3.4 15.8 1.0 C10 A:CUS1001 3.7 38.9 1.0 ND1 A:HIS64 4.1 18.3 1.0 O3 A:CUS1001 4.1 37.8 1.0 CG A:HIS64 4.2 15.4 1.0 C6 A:CUS1001 4.3 34.3 1.0 O A:HOH3112 4.4 55.0 1.0 C3 A:CUS1001 4.7 33.9 1.0 CB A:VAL68 4.8 16.0 1.0

S.Abe, T.Ueno, P.A.N.Reddy, S.Okazaki, T.Hikage, A.Suzuki, T.Yamane, H.Nakajima, Y.Watanabe. Design and Structure Analysis of Artificial Metalloproteins: Selective Coordination of HIS64 to Copper Complexes with Square-Planar Structure in the Apo-Myoglobin Scaffold Inorg.Chem. V. 46 5137 2007.
ISSN: ISSN 0020-1669
PubMed: 17523632
DOI: 10.1021/IC070289M