Copper in PDB 4eir: Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-2)

The structure of Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-2), PDB code: 4eir was solved by X.Li, W.T.Beeson, C.M.Phillips, M.A.Marletta, J.H.Cate, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.86 / 1.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.170, 41.990, 69.250, 90.00, 97.94, 90.00
R / Rfree (%)	13.2 / 14.9

The binding sites of Copper atom in the Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-2) (pdb code 4eir). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-2), PDB code: 4eir:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-2)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:10.2 occ:0.91 O A:HOH401 1.8 16.7 0.6 ND1 A:HIC1 1.9 10.9 1.0 NE2 A:HIS84 2.0 11.0 1.0 N A:HIC1 2.2 10.2 1.0 H2 A:HIC1 2.6 9.9 1.0 H A:HIC1 2.7 10.0 1.0 OH A:TYR168 2.8 10.3 1.0 CG A:HIC1 2.9 9.6 1.0 CD2 A:HIS84 3.0 10.9 1.0 CE1 A:HIC1 3.0 11.5 1.0 O1 A:OXY302 3.0 16.8 0.8 CE1 A:HIS84 3.0 12.0 1.0 HD2 A:HIS84 3.2 10.8 1.0 CA A:HIC1 3.2 8.9 1.0 HE1 A:HIC1 3.2 12.6 1.0 HH A:TYR168 3.2 10.0 1.0 HE1 A:HIS84 3.3 12.9 1.0 HB3 A:HIC1 3.3 10.1 1.0 CB A:HIC1 3.3 9.7 1.0 HA A:HIC1 3.6 8.9 1.0 OE1 A:GLN166 3.6 13.0 1.0 O B:HOH701 3.8 22.5 0.5 CZ A:TYR168 3.8 9.1 1.0 H2 B:GOL304 3.9 19.6 0.8 O2 A:OXY302 4.0 22.2 0.7 O A:HOH563 4.0 26.5 1.0 CD2 A:HIC1 4.1 10.1 1.0 NE2 A:HIC1 4.1 11.0 1.0 ND1 A:HIS84 4.1 12.3 1.0 CG A:HIS84 4.1 11.2 1.0 O A:HOH409 4.2 12.7 1.0 HE1 A:HIS157 4.3 12.6 1.0 HB2 A:HIC1 4.4 9.6 1.0 OE1 B:GLU30 4.4 17.7 0.5 HE1 A:TYR168 4.4 8.2 1.0 C A:HIC1 4.5 9.1 1.0 HE2 A:TYR168 4.5 8.6 1.0 CE1 A:TYR168 4.5 8.3 1.0 O B:HOH701 4.5 23.6 0.5 HD3 A:PRO28 4.6 9.1 1.0 CE2 A:TYR168 4.6 9.0 1.0 CD A:GLN166 4.7 12.2 1.0 HG3 A:MET80 4.7 10.7 1.0 HE21 A:GLN166 4.8 14.8 0.0 O A:HIC1 4.9 9.7 1.0 HE2 A:HIS157 4.9 13.3 0.0

Copper binding site 2 out of 2 in the Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-2)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-2) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:9.7 occ:0.96 O B:HOH401 1.8 16.1 0.5 ND1 B:HIC1 1.9 10.4 1.0 NE2 B:HIS84 2.0 10.0 1.0 N B:HIC1 2.2 9.3 1.0 H2 B:HIC1 2.6 9.2 1.0 H B:HIC1 2.6 9.0 1.0 OH B:TYR168 2.8 9.4 1.0 CG B:HIC1 2.9 9.5 1.0 CD2 B:HIS84 2.9 9.8 1.0 O1 B:OXY302 2.9 18.6 0.8 CE1 B:HIC1 3.0 11.4 1.0 CE1 B:HIS84 3.0 10.6 1.0 HD2 B:HIS84 3.1 10.0 1.0 CA B:HIC1 3.2 8.6 1.0 HB3 B:HIC1 3.2 8.9 1.0 HE1 B:HIC1 3.3 12.2 1.0 CB B:HIC1 3.3 9.0 1.0 HE1 B:HIS84 3.3 12.7 1.0 HH B:TYR168 3.3 8.8 1.0 OE1 B:GLN166 3.5 12.7 1.0 HA B:HIC1 3.5 8.3 1.0 O A:HOH634 3.6 22.7 0.5 CZ B:TYR168 3.8 8.0 1.0 O2 B:OXY302 3.9 20.2 0.7 O B:HOH559 3.9 26.4 1.0 CD2 B:HIC1 4.0 10.0 1.0 H2 A:GOL304 4.1 23.6 0.8 NE2 B:HIC1 4.1 10.4 1.0 ND1 B:HIS84 4.1 10.9 1.0 CG B:HIS84 4.1 9.3 1.0 O B:HOH409 4.2 12.0 1.0 HE1 B:HIS157 4.3 11.5 1.0 O A:HOH634 4.3 22.3 0.5 OE1 A:GLU30 4.3 18.0 0.5 HB2 B:HIC1 4.3 8.9 1.0 HE1 B:TYR168 4.4 7.7 1.0 HE2 B:TYR168 4.5 7.6 1.0 C B:HIC1 4.5 8.2 1.0 CE1 B:TYR168 4.5 7.7 1.0 CE2 B:TYR168 4.5 7.8 1.0 HD3 B:PRO28 4.6 8.1 1.0 CD B:GLN166 4.6 11.5 1.0 HE21 B:GLN166 4.6 16.8 0.0 HG3 B:MET80 4.8 9.3 1.0 HE2 B:HIS157 4.9 12.6 0.0 O B:HIC1 4.9 8.9 1.0 HD1 B:HIS84 5.0 10.0 0.0

X.Li, W.T.Beeson, C.M.Phillips, M.A.Marletta, J.H.Cate. Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases. Structure V. 20 1051 2012.
ISSN: ISSN 0969-2126
PubMed: 22578542
DOI: 10.1016/J.STR.2012.04.002